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PDBsum entry 1qvi
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protein ligands metals Protein-protein interface(s) links
Contractile protein PDB id
1qvi

 

 

 

 

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Contents
Protein chains
806 a.a. *
141 a.a. *
155 a.a. *
Ligands
VO4-ADP
Metals
_MG ×2
_CA
Waters ×52
* Residue conservation analysis
PDB id:
1qvi
Name: Contractile protein
Title: Crystal structure of scallop myosin s1 in the pre-power stroke state to 2.6 angstrom resolution: flexibility and function in the head
Structure: Myosin heavy chain, striated muscle. Chain: a. Myosin regulatory light chain, striated adductor muscle. Chain: y. Synonym: r-lc. Myosin essential light chain, striated adductor muscle. Chain: z. Synonym: e-lc, sulfhydryl light chain, shlc
Source: Argopecten irradians. Organism_taxid: 31199. Organism_taxid: 31199
Biol. unit: Trimer (from PQS)
Resolution:
2.54Å     R-factor:   0.212     R-free:   0.266
Authors: S.Gourinath,D.M.Himmel,J.H.Brown,L.Reshetnikova,A.G.Szent-Gyrgyi, C.Cohen
Key ref:
S.Gourinath et al. (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. PubMed id: 14656445 DOI: 10.1016/j.str.2003.10.013
Date:
27-Aug-03     Release date:   16-Dec-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P24733  (MYS_ARGIR) -  Myosin heavy chain, striated muscle from Argopecten irradians
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1938 a.a.
806 a.a.
Protein chain
Pfam   ArchSchema ?
P13543  (MLR_ARGIR) -  Myosin regulatory light chain, striated adductor muscle from Argopecten irradians
Seq:
Struc: 		157 a.a.
141 a.a.
Protein chain
Pfam   ArchSchema ?
P07291  (MLE_ARGIR) -  Myosin essential light chain, striated adductor muscle from Argopecten irradians
Seq:
Struc: 		157 a.a.
155 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.str.2003.10.013 Structure 11:1621-1627 (2003)
PubMed id: 14656445  
 
 
Crystal structure of scallop Myosin s1 in the pre-power stroke state to 2.6 a resolution: flexibility and function in the head.
S.Gourinath, D.M.Himmel, J.H.Brown, L.Reshetnikova, A.G.Szent-Györgyi, C.Cohen.
 
  ABSTRACT  
 
We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 A resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called "pliant region" at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the "internally uncoupled" state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Stabilizing Interactions in the So-Called "Pliant Region"--the MD/Lever Arm Junction--in Scallop S1(A) Displayed here is a schematic comparison between the pliant regions of the chicken smooth muscle MDE-MgADP·AlF[4] structure (Dominguez et al., 1998) (gray, only the lever arm is shown) and scallop S1-MgADP·VO[4] (the lever arm and motor domain are shown). These structures are superimposed by fitting the residues (765-773) immediately N-terminal to the "pliant region." The pliant region is straight in all scallop S1 structures but is bent in the chicken smooth muscle crystal structure (Dominguez et al., 1998) (also see text). The lever arm heavy chain is shown as a ribbon diagram in purple, and the motor domain is shown schematically with its subdomains (the 50 kDa upper and lower subdomains in red and pink, the N-terminal subdomain in blue, the converter in green, and the pliant helix in yellow).(B) As in (A) but from a perpendicular view and also showing the scallop light chains schematically (ELC in magenta, and RLC in light blue).(C) Magnified view of the pliant region of scallop S1 (in the same orientation as in [B] and including the ELC in magenta) shows the side chain interactions that appear to restrain the scallop pliant region from bending (salt bridges in red dashed lines, van der Waals contacts in blue dashed lines). These interactions are absent from the smooth muscle MDE crystal structure as a result of amino acid sequence differences from scallop myosin.
 
  The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1621-1627) copyright 2003.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21152002 C.D.Williams, M.Regnier, and T.L.Daniel (2010).
Axial and radial forces of cross-bridges depend on lattice spacing.
  PLoS Comput Biol, 6, e1001018.  
21132353 G.Offer, and K.W.Ranatunga (2010).
Crossbridge and filament compliance in muscle: implications for tension generation and lever arm swing.
  J Muscle Res Cell Motil, 31, 245-265.  
20385833 M.Takano, T.P.Terada, and M.Sasai (2010).
Unidirectional Brownian motion observed in an in silico single molecule experiment of an actomyosin motor.
  Proc Natl Acad Sci U S A, 107, 7769-7774.  
20428469 D.Parker, Z.Bryant, and S.L.Delp (2009).
Coarse-Grained Structural Modeling of Molecular Motors Using Multibody Dynamics.
  Cell Mol Bioeng, 2, 366-374.  
18996395 D.R.Weiss, and M.Levitt (2009).
Can morphing methods predict intermediate structures?
  J Mol Biol, 385, 665-674.  
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
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.  
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.  
17628590 J.Bosch, S.Turley, C.M.Roach, T.M.Daly, L.W.Bergman, and W.G.Hol (2007).
The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery.
  J Mol Biol, 372, 77-88.
PDB code: 2qac
17956731 J.Ménétrey, P.Llinas, M.Mukherjea, H.L.Sweeney, and A.Houdusse (2007).
The structural basis for the large powerstroke of myosin VI.
  Cell, 131, 300-308.
PDB code: 2v26
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.  
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
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.  
16102537 E.A.Stauffer, J.D.Scarborough, M.Hirono, E.D.Miller, K.Shah, J.A.Mercer, J.R.Holt, and P.G.Gillespie (2005).
Fast adaptation in vestibular hair cells requires myosin-1c activity.
  Neuron, 47, 541-553.  
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 codes are shown on the right.

 

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