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Myosin PDB id
1b7t
Jmol
Contents
Protein chains
766 a.a. *
138 a.a. *
153 a.a. *
Ligands
ADP
Metals
_MG ×2
_CA
Waters ×104
* Residue conservation analysis
PDB id:
1b7t
Name: Myosin
Title: Myosin digested by papain
Structure: Myosin heavy chain. Chain: a. Fragment: papain digested, subfragment 1 (s1). Myosin regulatory light chain. Chain: y. Fragment: papain digested, subfragment 1 (s1). Myosin essential light chain. Chain: z. Fragment: papain digested, subfragment 1 (s1)
Source: Argopecten irradians. Organism_taxid: 31199. Tissue: skeletal muscle. Other_details: papain digestion of myosin. Other_details: papain digestion of myosin
Biol. unit: Trimer (from PQS)
Resolution:
2.50Å     R-factor:   0.224     R-free:   0.297
Authors: A.Houdusse,V.Kalabokis,D.Himmel,A.G.Szent-Gyorgyi,C.Cohen
Key ref:
A.Houdusse et al. (1999). Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell, 97, 459-470. PubMed id: 10338210 DOI: 10.1016/S0092-8674(00)80756-4
Date:
15-Jan-99     Release date:   12-May-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P24733  (MYS_AEQIR) -  Myosin heavy chain, striated muscle
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1938 a.a.
766 a.a.
Protein chain
Pfam   ArchSchema ?
P13543  (MLR_AEQIR) -  Myosin regulatory light chain, striated adductor muscle
Seq:
Struc: 		157 a.a.
138 a.a.
Protein chain
Pfam  
P07291  (MLE_AEQIR) -  Myosin essential light chain, striated adductor muscle
Seq:
Struc: 		157 a.a.
153 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     myosin complex   1 term 
  Biochemical function     calcium ion binding     3 terms  

 

 
DOI no: 10.1016/S0092-8674(00)80756-4 Cell 97:459-470 (1999)
PubMed id: 10338210  
 
 
Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.
A.Houdusse, V.N.Kalabokis, D.Himmel, A.G.Szent-Györgyi, C.Cohen.
 
  ABSTRACT  
 
The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre-power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible "joints" produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis ("ATP") states of the contractile cycle in which the myosin heads stay detached from actin.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. The ELC/Converter Interactions Modulate the Position of the Lever ArmDifferent positions of the converter in the three states result in major movements of the lever arm (see Figure 1 and Figure 2). This diagram illustrates how the converter and the ELC interact differently in chicken S1 (A), scallop S1 complexed with MgADP (B), and smooth MDE–AlF[4]^− (C). In this view, the converter (green) and the HP helix (yellow) appear to be in similar positions. Note that differences in the interactions between the C-terminal lobe of the ELC (pink) and the motor domain in these structures result in different bending of the heavy chain helix (cyan) after the first three turns (green) that are part of the converter.
Figure 5.
Figure 5. The Relay Controls the Position of the Converter to which It Is Linked by Strong Conserved InteractionsRibbon diagram of the interface between the relay (yellow) and the converter (β sheet and last helix in green) in chicken S1 (A), scallop S1 complexed with MgADP (B), and smooth MDE–AlF[4]^− (C) oriented so that the converters superimpose. Note that the orientation of the last three turns of the HP helix (yellow) is similar in all these structures, since three glutamate residues of this helix (brown) interact with residues of the converter (cyan) in all three states. In contrast, the conformation of the loop of the relay (yellow) is very different and is most rigid in (C) where it interacts with the SH1 helix (red). Conformational changes at both ends of the relay allow the orientation of the lower 50 kDa subdomain (white, HP and HQ helices) to differ with respect to that of the converter in these three states. Note also how the environment around the tryptophane residue (blue) of the relay varies in the three states.
 
  The above figures are reprinted by permission from Cell Press: Cell (1999, 97, 459-470) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21326200 C.Veigel, and C.F.Schmidt (2011).
Moving into the cell: single-molecule studies of molecular motors in complex environments.
  Nat Rev Mol Cell Biol, 12, 163-176.  
21310275 D.M.Jordan, A.Kiezun, S.M.Baxter, V.Agarwala, R.C.Green, M.F.Murray, T.Pugh, M.S.Lebo, H.L.Rehm, B.H.Funke, and S.R.Sunyaev (2011).
Development and validation of a computational method for assessment of missense variants in hypertrophic cardiomyopathy.
  Am J Hum Genet, 88, 183-192.  
21149681 J.H.Brown, V.S.Kumar, E.O'Neall-Hennessey, L.Reshetnikova, H.Robinson, M.Nguyen-McCarty, A.G.Szent-Györgyi, and C.Cohen (2011).
Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.
  Proc Natl Acad Sci U S A, 108, 114-119.
PDB code: 3pn7
21421313 S.Masuda, T.Tomohiro, and Y.Hatanaka (2011).
Rapidly photoactivatable ATP probes for specific labeling of tropomyosin within the actomyosin protein complex.
  Bioorg Med Chem Lett, 21, 2252-2254.  
21245357 Y.E.Nesmelov, R.V.Agafonov, I.V.Negrashov, S.E.Blakely, M.A.Titus, and D.D.Thomas (2011).
Structural kinetics of myosin by transient time-resolved FRET.
  Proc Natl Acad Sci U S A, 108, 1891-1896.  
20192767 H.L.Sweeney, and A.Houdusse (2010).
Structural and functional insights into the Myosin motor mechanism.
  Annu Rev Biophys, 39, 539-557.  
20656787 J.T.Granados-Riveron, T.K.Ghosh, M.Pope, F.Bu'Lock, C.Thornborough, J.Eason, E.P.Kirk, D.Fatkin, M.P.Feneley, R.P.Harvey, J.A.Armour, and J.David Brook (2010).
Alpha-cardiac myosin heavy chain (MYH6) mutations affecting myofibril formation are associated with congenital heart defects.
  Hum Mol Genet, 19, 4007-4016.  
20687691 K.Amano, T.Yoshidome, M.Iwaki, M.Suzuki, and M.Kinoshita (2010).
Entropic potential field formed for a linear-motor protein near a filament: Statistical-mechanical analyses using simple models.
  J Chem Phys, 133, 045103.  
19853615 V.Ovchinnikov, B.L.Trout, and M.Karplus (2010).
Mechanical coupling in myosin V: a simulation study.
  J Mol Biol, 395, 815-833.  
19651039 B.Seebohm, F.Matinmehr, J.Köhler, A.Francino, F.Navarro-Lopéz, A.Perrot, C.Ozcelik, W.J.McKenna, B.Brenner, and T.Kraft (2009).
Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance.
  Biophys J, 97, 806-824.  
19408946 K.Ajtai, M.F.Halstead, M.Nyitrai, A.R.Penheiter, Y.Zheng, and T.P.Burghardt (2009).
The myosin C-loop is an allosteric actin contact sensor in actomyosin.
  Biochemistry, 48, 5263-5275.  
19289039 W.Zheng, and D.Thirumalai (2009).
Coupling between normal modes drives protein conformational dynamics: illustrations using allosteric transitions in myosin II.
  Biophys J, 96, 2128-2137.  
18957515 A.J.Engler, C.Carag-Krieger, C.P.Johnson, M.Raab, H.Y.Tang, D.W.Speicher, J.W.Sanger, J.M.Sanger, and D.E.Discher (2008).
Embryonic cardiomyocytes beat best on a matrix with heart-like elasticity: scar-like rigidity inhibits beating.
  J Cell Sci, 121, 3794-3802.  
18059020 A.Pecci, E.Panza, N.Pujol-Moix, C.Klersy, F.Di Bari, V.Bozzi, P.Gresele, S.Lethagen, F.Fabris, C.Dufour, A.Granata, M.Doubek, C.Pecoraro, P.A.Koivisto, P.G.Heller, A.Iolascon, P.Alvisi, D.Schwabe, E.De Candia, B.Rocca, U.Russo, U.Ramenghi, P.Noris, M.Seri, C.L.Balduini, and A.Savoia (2008).
Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations predicts the natural history of MYH9-related disease.
  Hum Mutat, 29, 409-417.  
18805936 A.R.Thompson, N.Naber, C.Wilson, R.Cooke, and D.D.Thomas (2008).
Structural dynamics of the actomyosin complex probed by a bifunctional spin label that cross-links SH1 and SH2.
  Biophys J, 95, 5238-5246.  
19325727 I.Aprodu, A.Redaelli, and M.Soncini (2008).
Actomyosin interaction: mechanical and energetic properties in different nucleotide binding States.
  Int J Mol Sci, 9, 1927-1943.  
18155233 J.H.Brown, Y.Yang, L.Reshetnikova, S.Gourinath, D.Süveges, J.Kardos, F.Hóbor, R.Reutzel, L.Nyitray, and C.Cohen (2008).
An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins.
  J Mol Biol, 375, 1434-1443.
PDB codes: 3bas 3bat
18951904 L.Alamo, W.Wriggers, A.Pinto, F.Bártoli, L.Salazar, F.Q.Zhao, R.Craig, and R.Padrón (2008).
Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.
  J Mol Biol, 384, 780-797.
PDB code: 3dtp
18704171 M.Cecchini, A.Houdusse, and M.Karplus (2008).
Allosteric communication in myosin V: from small conformational changes to large directed movements.
  PLoS Comput Biol, 4, e1000129.  
18568345 M.J.Harris, and H.J.Woo (2008).
Energetics of subdomain movements and fluorescence probe solvation environment change in ATP-bound myosin.
  Eur Biophys J, 38, 1.  
18849419 R.Shi, M.Pineda, E.Ajamian, Q.Cui, A.Matte, and M.Cygler (2008).
Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
  J Bacteriol, 190, 8137-8144.
PDB codes: 3cqh 3cqi 3cqj 3cqk
18616971 S.L.Hooper, K.H.Hobbs, and J.B.Thuma (2008).
Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.
  Prog Neurobiol, 86, 72.  
18462751 W.A.Kronert, C.M.Dambacher, A.F.Knowles, D.M.Swank, and S.I.Bernstein (2008).
Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function.
  J Mol Biol, 379, 443-456.  
17709338 A.Schlessinger, M.Punta, and B.Rost (2007).
Natively unstructured regions in proteins identified from contact predictions.
  Bioinformatics, 23, 2376-2384.  
17502095 C.R.Bagshaw (2007).
Myosin mechanochemistry.
  Structure, 15, 511-512.  
17541712 L.Shakirova, V.Mikhailova, E.Siletskaya, V.P.Timofeev, and D.I.Levitsky (2007).
Nucleotide-induced and actin-induced structural changes in SH1-SH2-modified myosin subfragment 1.
  J Muscle Res Cell Motil, 28, 67-78.  
17704147 M.F.Halstead, K.Ajtai, A.R.Penheiter, J.D.Spencer, Y.Zheng, E.A.Morrison, and T.P.Burghardt (2007).
An unusual transduction pathway in human tonic smooth muscle myosin.
  Biophys J, 93, 3555-3566.  
17617722 M.Suzuki, S.Sakuda, and H.Nagasawa (2007).
Identification of chitin in the prismatic layer of the shell and a chitin synthase gene from the Japanese pearl oyster, Pinctada fucata.
  Biosci Biotechnol Biochem, 71, 1735-1744.  
17142278 N.M.Kad, J.B.Patlak, P.M.Fagnant, K.M.Trybus, and D.M.Warshaw (2007).
Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.
  Biophys J, 92, 1623-1631.  
17900617 S.Tang, J.C.Liao, A.R.Dunn, R.B.Altman, J.A.Spudich, and J.P.Schmidt (2007).
Predicting allosteric communication in myosin via a pathway of conserved residues.
  J Mol Biol, 373, 1361-1373.  
17913331 T.P.Burghardt, J.Y.Hu, and K.Ajtai (2007).
Myosin dynamics on the millisecond time scale.
  Biophys Chem, 131, 15-28.  
17502101 Y.Yang, S.Gourinath, M.Kovács, L.Nyitray, R.Reutzel, D.M.Himmel, E.O'Neall-Hennessey, L.Reshetnikova, A.G.Szent-Györgyi, J.H.Brown, and C.Cohen (2007).
Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor.
  Structure, 15, 553-564.
PDB codes: 2ec6 2ekv 2ekw 2os8 2otg 2ovk 2oy6 3i5f 3i5g 3i5h 3i5i
16907132 B.Geislinger, and R.Kawai (2006).
Brownian molecular motors driven by rotation-translation coupling.
  Phys Rev E Stat Nonlin Soft Matter Phys, 74, 011912.  
17012238 B.Salzameda, K.C.Facemyer, B.W.Beck, and C.R.Cremo (2006).
The N-terminal lobes of both regulatory light chains interact with the tail domain in the 10 S-inhibited conformation of smooth muscle myosin.
  J Biol Chem, 281, 38801-38811.  
16963511 G.Lan, and S.X.Sun (2006).
Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI.
  Biophys J, 91, 4002-4013.  
16500969 M.Iwaki, H.Tanaka, A.H.Iwane, E.Katayama, M.Ikebe, and T.Yanagida (2006).
Cargo-binding makes a wild-type single-headed myosin-VI move processively.
  Biophys J, 90, 3643-3652.  
17013387 M.Tomishige, N.Stuurman, and R.D.Vale (2006).
Single-molecule observations of neck linker conformational changes in the kinesin motor protein.
  Nat Struct Mol Biol, 13, 887-894.  
16901894 S.Iwai, D.Hanamoto, and S.Chaen (2006).
A point mutation in the SH1 helix alters elasticity and thermal stability of myosin II.
  J Biol Chem, 281, 30736-30744.  
16547732 S.Nikolaou, M.Hu, N.B.Chilton, D.Hartman, A.J.Nisbet, P.J.Presidente, and R.B.Gasser (2006).
Isolation and characterization of class II myosin genes from Haemonchus contortus.
  Parasitol Res, 99, 200-203.  
16645962 Y.Liu, M.Scolari, W.Im, and H.J.Woo (2006).
Protein-protein interactions in actin-myosin binding and structural effects of R405Q mutation: a molecular dynamics study.
  Proteins, 64, 156-166.  
16844693 Z.E.Sauna, K.Nandigama, and S.V.Ambudkar (2006).
Exploiting reaction intermediates of the ATPase reaction to elucidate the mechanism of transport by P-glycoprotein (ABCB1).
  J Biol Chem, 281, 26501-26511.  
15951390 C.I.Robertson, D.P.Gaffney, L.R.Chrin, and C.L.Berger (2005).
Structural rearrangements in the active site of smooth-muscle myosin.
  Biophys J, 89, 1882-1892.  
16383662 H.J.Woo, and C.L.Moss (2005).
Analytical theory of the stochastic dynamics of the power stroke in nonprocessive motor proteins.
  Phys Rev E Stat Nonlin Soft Matter Phys, 72, 051924.  
15944696 J.Ménétrey, A.Bahloul, A.L.Wells, C.M.Yengo, C.A.Morris, H.L.Sweeney, and A.Houdusse (2005).
The structure of the myosin VI motor reveals the mechanism of directionality reversal.
  Nature, 435, 779-785.
PDB codes: 2bkh 2bki
15642268 M.A.Ferenczi, S.Y.Bershitsky, N.Koubassova, V.Siththanandan, W.I.Helsby, P.Panine, M.Roessle, T.Narayanan, and A.K.Tsaturyan (2005).
The "roll and lock" mechanism of force generation in muscle.
  Structure, 13, 131-141.  
15768443 P.Chen, and L.Zhang (2005).
New evidences of glass transitions and microstructures of soy protein plasticized with glycerol.
  Macromol Biosci, 5, 237-245.  
16143997 P.Chen, L.Zhang, and F.Cao (2005).
Effects of moisture on glass transition and microstructure of glycerol-plasticized soy protein.
  Macromol Biosci, 5, 872-880.  
15255774 C.Mavroidis, A.Dubey, and M.L.Yarmush (2004).
Molecular machines.
  Annu Rev Biomed Eng, 6, 363-395.  
15627371 D.I.Levitsky (2004).
Actomyosin systems of biological motility.
  Biochemistry (Mosc), 69, 1177-1189.  
15647166 D.J.Manstein (2004).
Molecular engineering of myosin.
  Philos Trans R Soc Lond B Biol Sci, 359, 1907-1912.  
15579689 D.P.Kiehart, J.D.Franke, M.K.Chee, R.A.Montague, T.L.Chen, J.Roote, and M.Ashburner (2004).
Drosophila crinkled, mutations of which disrupt morphogenesis and cause lethality, encodes fly myosin VIIA.
  Genetics, 168, 1337-1352.  
15184651 D.Risal, S.Gourinath, D.M.Himmel, A.G.Szent-Györgyi, and C.Cohen (2004).
Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding.
  Proc Natl Acad Sci U S A, 101, 8930-8935.
PDB codes: 1s5g 1sr6
15473855 F.Buss, G.Spudich, and J.Kendrick-Jones (2004).
Myosin VI: cellular functions and motor properties.
  Annu Rev Cell Dev Biol, 20, 649-676.  
15647159 H.L.Sweeney, and A.Houdusse (2004).
The motor mechanism of myosin V: insights for muscle contraction.
  Philos Trans R Soc Lond B Biol Sci, 359, 1829-1841.  
15044955 I.Lister, S.Schmitz, M.Walker, J.Trinick, F.Buss, C.Veigel, and J.Kendrick-Jones (2004).
A monomeric myosin VI with a large working stroke.
  EMBO J, 23, 1729-1738.  
14747987 I.Navizet, R.Lavery, and R.L.Jernigan (2004).
Myosin flexibility: structural domains and collective vibrations.
  Proteins, 54, 384-393.  
15189875 J.D.Lawson, E.Pate, I.Rayment, and R.G.Yount (2004).
Molecular dynamics analysis of structural factors influencing back door pi release in myosin.
  Biophys J, 86, 3794-3803.  
15711883 J.Van Dijk, C.Lafont, M.L.Knetsch, J.Derancourt, D.J.Manstein, E.C.Long, and P.Chaussepied (2004).
Conformational changes in actin-myosin isoforms probed by Ni(II).Gly-Gly-His reactivity.
  J Muscle Res Cell Motil, 25, 527-537.  
15020589 K.Ajtai, S.P.Garamszegi, S.Watanabe, M.Ikebe, and T.P.Burghardt (2004).
The myosin cardiac loop participates functionally in the actomyosin interaction.
  J Biol Chem, 279, 23415-23421.  
15510214 P.D.Coureux, H.L.Sweeney, and A.Houdusse (2004).
Three myosin V structures delineate essential features of chemo-mechanical transduction.
  EMBO J, 23, 4527-4537.
PDB codes: 1w7i 1w7j 1w8j
15647169 R.Roberts, I.Lister, S.Schmitz, M.Walker, C.Veigel, J.Trinick, F.Buss, and J.Kendrick-Jones (2004).
Myosin VI: cellular functions and motor properties.
  Philos Trans R Soc Lond B Biol Sci, 359, 1931-1944.  
15647164 V.Lombardi, G.Piazzesi, M.Reconditi, M.Linari, L.Lucii, A.Stewart, Y.B.Sun, P.Boesecke, T.Narayanan, T.Irving, and M.Irving (2004).
X-ray diffraction studies of the contractile mechanism in single muscle fibres.
  Philos Trans R Soc Lond B Biol Sci, 359, 1883-1893.  
15647167 Y.Takagi, H.Shuman, and Y.E.Goldman (2004).
Coupling between phosphate release and force generation in muscle actomyosin.
  Philos Trans R Soc Lond B Biol Sci, 359, 1913-1920.  
12466270 A.Inoue, and M.Ikebe (2003).
Characterization of the motor activity of mammalian myosin VIIA.
  J Biol Chem, 278, 5478-5487.  
12547786 A.Muhlrad, Y.M.Peyser, M.Nili, K.Ajtai, E.Reisler, and T.P.Burghardt (2003).
Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever-arm movement.
  Biophys J, 84, 1047-1056.  
12719468 D.Köhler, C.Ruff, E.Meyhöfer, and M.Bähler (2003).
Different degrees of lever arm rotation control myosin step size.
  J Cell Biol, 161, 237-241.  
12885653 H.A.AL-Khayat, L.Hudson, M.K.Reedy, T.C.Irving, and J.M.Squire (2003).
Myosin head configuration in relaxed insect flight muscle: x-ray modeled resting cross-bridges in a pre-powerstroke state are poised for actin binding.
  Biophys J, 85, 1063-1079.  
12668452 J.Borejdo, and I.Akopova (2003).
Orientational changes of crossbridges during single turnover of ATP.
  Biophys J, 84, 2450-2459.  
12756255 K.Ito, T.Q.Uyeda, Y.Suzuki, K.Sutoh, and K.Yamamoto (2003).
Requirement of domain-domain interaction for conformational change and functional ATP hydrolysis in myosin.
  J Biol Chem, 278, 31049-31057.  
12885652 M.Nyitrai, W.F.Stafford, A.G.Szent-Györgyi, and M.A.Geeves (2003).
Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin.
  Biophys J, 85, 1053-1062.  
12679807 M.Xiao, J.G.Reifenberger, A.L.Wells, C.Baldacchino, L.Q.Chen, P.Ge, H.L.Sweeney, and P.R.Selvin (2003).
An actin-dependent conformational change in myosin.
  Nat Struct Biol, 10, 402-408.  
14508494 P.D.Coureux, A.L.Wells, J.Ménétrey, C.M.Yengo, C.A.Morris, H.L.Sweeney, and A.Houdusse (2003).
A structural state of the myosin V motor without bound nucleotide.
  Nature, 425, 419-423.
PDB code: 1oe9
  14656445 S.Gourinath, D.M.Himmel, J.H.Brown, L.Reshetnikova, A.G.Szent-Györgyi, and C.Cohen (2003).
Crystal structure of scallop Myosin s1 in the pre-power stroke state to 2.6 a resolution: flexibility and function in the head.
  Structure, 11, 1621-1627.
PDB code: 1qvi
14502270 T.F.Reubold, S.Eschenburg, A.Becker, F.J.Kull, and D.J.Manstein (2003).
A structural model for actin-induced nucleotide release in myosin.
  Nat Struct Biol, 10, 826-830.
PDB code: 1q5g
14580214 Y.M.Peyser, S.Shaya, K.Ajtai, T.P.Burghardt, and A.Muhlrad (2003).
Cosolvent-induced aggregation inhibits myosin ATPase activity by stabilizing the predominant transition intermediate.
  Biochemistry, 42, 12669-12675.  
11959853 C.M.Yengo, E.M.De La Cruz, L.R.Chrin, D.P.Gaffney, and C.L.Berger (2002).
Actin-induced closure of the actin-binding cleft of smooth muscle myosin.
  J Biol Chem, 277, 24114-24119.  
12297624 D.M.Himmel, S.Gourinath, L.Reshetnikova, Y.Shen, A.G.Szent-Györgyi, and C.Cohen (2002).
Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.
  Proc Natl Acad Sci U S A, 99, 12645-12650.
PDB codes: 1kk7 1kk8 1kqm 1kwo 1l2o
11792544 H.Higuchi, and S.A.Endow (2002).
Directionality and processivity of molecular motors.
  Curr Opin Cell Biol, 14, 50-57.  
11916868 J.Gu, S.Xu, and L.C.Yu (2002).
A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle.
  Biophys J, 82, 2123-2133.  
11904418 J.Köhler, G.Winkler, I.Schulte, T.Scholz, W.McKenna, B.Brenner, and T.Kraft (2002).
Mutation of the myosin converter domain alters cross-bridge elasticity.
  Proc Natl Acad Sci U S A, 99, 3557-3562.  
12414706 L.K.Nitao, T.O.Yeates, and E.Reisler (2002).
Conformational dynamics of the SH1-SH2 helix in the transition states of myosin subfragment-1.
  Biophys J, 83, 2733-2741.  
12124286 M.G.Bell, R.E.Dale, U.A.van der Heide, and Y.E.Goldman (2002).
Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges.
  Biophys J, 83, 1050-1073.  
11810692 M.J.Tyska, and D.M.Warshaw (2002).
The myosin power stroke.
  Cell Motil Cytoskeleton, 51, 1.  
12032065 M.Kollmar, U.Dürrwang, W.Kliche, D.J.Manstein, and F.J.Kull (2002).
Crystal structure of the motor domain of a class-I myosin.
  EMBO J, 21, 2517-2525.
PDB code: 1lkx
11985595 N.Hartvig, D.Lõrinczy, N.Farkas, and J.Belagyi (2002).
Effect of adenosine 5'-[beta,gamma-imido]triphosphate on myosin head domain movements.
  Eur J Biochem, 269, 2168-2177.  
11867464 R.W.Kensler (2002).
Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.
  Biophys J, 82, 1497-1508.  
12499355 S.Burgess, M.Walker, F.Wang, J.R.Sellers, H.D.White, P.J.Knight, and J.Trinick (2002).
The prepower stroke conformation of myosin V.
  J Cell Biol, 159, 983-991.  
11814335 S.Park, and T.P.Burghardt (2002).
Tyrosine mediated tryptophan ATP sensitivity in skeletal myosin.
  Biochemistry, 41, 1436-1444.  
12441389 S.R.Martin, and P.M.Bayley (2002).
Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V.
  Protein Sci, 11, 2909-2923.  
11806909 T.J.Minehardt, N.Marzari, R.Cooke, E.Pate, P.A.Kollman, and R.Car (2002).
A classical and ab initio study of the interaction of the myosin triphosphate binding domain with ATP.
  Biophys J, 82, 660-675.  
11880367 T.Masaike, E.Muneyuki, H.Noji, K.Kinosita, and M.Yoshida (2002).
F1-ATPase changes its conformations upon phosphate release.
  J Biol Chem, 277, 21643-21649.  
12082180 T.P.Terada, M.Sasai, and T.Yomo (2002).
Conformational change of the actomyosin complex drives the multiple stepping movement.
  Proc Natl Acad Sci U S A, 99, 9202-9206.  
12220198 W.Bernt, K.Polosukhina, B.Weiner, W.Tscharnuter, and S.Highsmith (2002).
Active site control of myosin cross-bridge zeta potential.
  Biochemistry, 41, 11308-11314.  
11297926 A.Houdusse, and H.L.Sweeney (2001).
Myosin motors: missing structures and hidden springs.
  Curr Opin Struct Biol, 11, 182-194.  
11425314 B.A.Baumann, B.D.Hambly, K.Hideg, and P.G.Fajer (2001).
The regulatory domain of the myosin head behaves as a rigid lever.
  Biochemistry, 40, 7868-7873.  
11387196 M.Yun, X.Zhang, C.G.Park, H.W.Park, and S.A.Endow (2001).
A structural pathway for activation of the kinesin motor ATPase.
  EMBO J, 20, 2611-2618.
PDB codes: 1f9t 1f9u 1f9v 1f9w
11163130 T.Hasson, and R.E.Cheney (2001).
Mechanisms of motor protein reversal.
  Curr Opin Cell Biol, 13, 29-35.  
11222280 T.J.Minehardt, R.Cooke, E.Pate, and P.A.Kollman (2001).
Molecular dynamics study of the energetic, mechanistic, and structural implications of a closed phosphate tube in ncd.
  Biophys J, 80, 1151-1168.  
11294650 T.P.Burghardt, A.R.Cruz-Walker, S.Park, and K.Ajtai (2001).
Conformation of myosin interdomain interactions during contraction: deductions from muscle fibers using polarized fluorescence.
  Biochemistry, 40, 4821-4833.  
11294651 T.P.Burghardt, S.Park, and K.Ajtai (2001).
Conformation of myosin interdomain interactions during contraction: deductions from proteins in solution.
  Biochemistry, 40, 4834-4843.  
11287639 T.Wendt, D.Taylor, K.M.Trybus, and K.Taylor (2001).
Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2.
  Proc Natl Acad Sci U S A, 98, 4361-4366.
PDB code: 1i84
11226153 W.Kliche, S.Fujita-Becker, M.Kollmar, D.J.Manstein, and F.J.Kull (2001).
Structure of a genetically engineered molecular motor.
  EMBO J, 20, 40-46.
PDB code: 1g8x
11163129 W.R.Schief, and J.Howard (2001).
Conformational changes during kinesin motility.
  Curr Opin Cell Biol, 13, 19-28.  
11251058 Y.B.Sun, K.Hilber, and M.Irving (2001).
Effect of active shortening on the rate of ATP utilisation by rabbit psoas muscle fibres.
  J Physiol, 531, 781-791.  
  11356282 Y.Ishii, A.Ishijima, and T.Yanagida (2001).
Single molecule nanomanipulation of biomolecules.
  Trends Biotechnol, 19, 211-216.  
11463651 Y.M.Peyser, K.Ajtai, T.P.Burghardt, and A.Muhlrad (2001).
Effect of ionic strength on the conformation of myosin subfragment 1-nucleotide complexes.
  Biophys J, 81, 1101-1114.  
10866971 A.A.Bobkov, and E.Reisler (2000).
Is SH1-SH2-cross-linked myosin subfragment 1 a structural analog of the weakly-bound state of myosin?
  Biophys J, 79, 460-467.  
11016966 A.Houdusse, A.G.Szent-Gyorgyi, and C.Cohen (2000).
Three conformational states of scallop myosin S1.
  Proc Natl Acad Sci U S A, 97, 11238-11243.
PDB codes: 1dfk 1dfl
  11023810 A.K.Lalwani, J.A.Goldstein, M.J.Kelley, W.Luxford, C.M.Castelein, and A.N.Mhatre (2000).
Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in nonmuscle myosin MYH9.
  Am J Hum Genet, 67, 1121-1128.  
11123942 A.Málnási-Csizmadia, R.J.Woolley, and C.R.Bagshaw (2000).
Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography.
  Biochemistry, 39, 16135-16146.  
10617631 A.M.Gulick, C.B.Bauer, J.B.Thoden, E.Pate, R.G.Yount, and I.Rayment (2000).
X-ray structures of the Dictyostelium discoideum myosin motor domain with six non-nucleotide analogs.
  J Biol Chem, 275, 398-408.
PDB codes: 1d0x 1d0y 1d0z 1d1a 1d1b 1d1c
10962092 B.Pliszka, E.Karczewska, and B.Wawro (2000).
Nucleotide-induced movements in the myosin head near the converter region.
  Biochim Biophys Acta, 1481, 55-62.  
11087368 E.M.De La Cruz, A.L.Wells, H.L.Sweeney, and E.M.Ostap (2000).
Actin and light chain isoform dependence of myosin V kinetics.
  Biochemistry, 39, 14196-14202.  
10618387 E.W.Becker (2000).
Kinetic equilibrium of forces and molecular events in muscle contraction.
  Proc Natl Acad Sci U S A, 97, 157-161.  
11016961 H.Onishi, K.Konishi, K.Fujiwara, K.Hayakawa, M.Tanokura, H.M.Martinez, and M.F.Morales (2000).
On the tryptophan residue of smooth muscle myosin that responds to binding of nucleotide.
  Proc Natl Acad Sci U S A, 97, 11203-11208.  
10671524 H.Patel, S.S.Margossian, and P.D.Chantler (2000).
Locking regulatory myosin in the off-state with trifluoperazine.
  J Biol Chem, 275, 4880-4888.  
10692329 J.J.MacLean, L.R.Chrin, and C.L.Berger (2000).
Dynamics at Lys-553 of the acto-myosin interface in the weakly and strongly bound states.
  Biophys J, 78, 1441-1448.  
10969011 J.Xu, and D.D.Root (2000).
Conformational selection during weak binding at the actin and myosin interface.
  Biophys J, 79, 1498-1510.  
10677484 K.Konno, K.Ue, M.Khoroshev, H.Martinez, B.Ray, and M.F.Morales (2000).
Consequences of placing an intramolecular crosslink in myosin S1.
  Proc Natl Acad Sci U S A, 97, 1461-1466.  
10827984 L.K.Nitao, and E.Reisler (2000).
Actin and temperature effects on the cross-linking of the SH1-SH2 helix in myosin subfragment 1.
  Biophys J, 78, 3072-3080.  
10684610 M.Tiepold, W.Kliche, J.Pfannstiel, and H.Faulstich (2000).
Stepwise modulation of ATPase activity, nucleotide trapping, and sliding motility of myosin S1 by modification of the thiol region with residues of increasing size.
  Biochemistry, 39, 1305-1315.  
10679363 N.Volkmann, and D.Hanein (2000).
Actomyosin: law and order in motility.
  Curr Opin Cell Biol, 12, 26-34.  
10809750 P.A.Ellison, J.R.Sellers, and C.R.Cremo (2000).
Kinetics of smooth muscle heavy meromyosin with one thiophosphorylated head.
  J Biol Chem, 275, 15142-15151.  
10679320 R.A.Cross (2000).
Molecular motors: Kinesin's dynamically dockable neck.
  Curr Biol, 10, R124-R126.  
10679326 R.B.Case, S.Rice, C.L.Hart, B.Ly, and R.D.Vale (2000).
Role of the kinesin neck linker and catalytic core in microtubule-based motility.
  Curr Biol, 10, 157-160.  
10753125 R.D.Vale, and R.A.Milligan (2000).
The way things move: looking under the hood of molecular motor proteins.
  Science, 288, 88-95.  
11015212 S.Highsmith, K.Polosukhina, and D.Eden (2000).
Myosin motor domain lever arm rotation is coupled to ATP hydrolysis.
  Biochemistry, 39, 12330-12335.  
11012667 S.Quevillon-Chéruel, C.Janmot, M.Nozais, A.M.Lompré, and J.J.Béchet (2000).
Functional regions in the essential light chain of smooth muscle myosin as revealed by the mutagenesis approach.
  Eur J Biochem, 267, 6151-6157.  
11114175 T.Martinsson, A.Oldfors, N.Darin, K.Berg, H.Tajsharghi, M.Kyllerman, and J.Wahlstrom (2000).
Autosomal dominant myopathy: missense mutation (Glu-706 --> Lys) in the myosin heavy chain IIa gene.
  Proc Natl Acad Sci U S A, 97, 14614-14619.  
10679365 T.Yanagida, K.Kitamura, H.Tanaka, A.Hikikoshi Iwane, and S.Esaki (2000).
Single molecule analysis of the actomyosin motor.
  Curr Opin Cell Biol, 12, 20-25.  
11007486 W.M.Shih, Z.Gryczynski, J.R.Lakowicz, and J.A.Spudich (2000).
A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin.
  Cell, 102, 683-694.  
10545173 C.M.Yengo, L.Chrin, A.S.Rovner, and C.L.Berger (1999).
Intrinsic tryptophan fluorescence identifies specific conformational changes at the actomyosin interface upon actin binding and ADP release.
  Biochemistry, 38, 14515-14523.  
10563790 J.Van Dijk, M.Furch, C.Lafont, D.J.Manstein, and P.Chaussepied (1999).
Functional characterization of the secondary actin binding site of myosin II.
  Biochemistry, 38, 15078-15085.  
10571184 K.A.Taylor, H.Schmitz, M.C.Reedy, Y.E.Goldman, C.Franzini-Armstrong, H.Sasaki, R.T.Tregear, K.Poole, C.Lucaveche, R.J.Edwards, L.F.Chen, H.Winkler, and M.K.Reedy (1999).
Tomographic 3D reconstruction of quick-frozen, Ca2+-activated contracting insect flight muscle.
  Cell, 99, 421-431.  
10531021 R.Cooke (1999).
Myosin structure: does the tail wag the dog?
  Curr Biol, 9, R773-R775.  
10611679 R.D.Vale (1999).
Millennial musings on molecular motors.
  Trends Cell Biol, 9, M38-M42.  
10545367 S.Xu, J.Gu, T.Rhodes, B.Belknap, G.Rosenbaum, G.Offer, H.White, and L.C.Yu (1999).
The M.ADP.P(i) state is required for helical order in the thick filaments of skeletal muscle
  Biophys J, 77, 2665-2676.  
10704189 T.B.Friedman, J.R.Sellers, and K.B.Avraham (1999).
Unconventional myosins and the genetics of hearing loss.
  Am J Med Genet, 89, 147-157.  
10506171 T.Hiratsuka (1999).
ATP-induced opposite changes in the local environments around Cys(697) (SH2) and Cys(707) (SH1) of the myosin motor domain revealed by the prodan fluorescence.
  J Biol Chem, 274, 29156-29163.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.