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PDBsum entry 1o1d
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protein Protein-protein interface(s) links
Contractile protein PDB id
1o1d

 

 

 

 

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Contents
Protein chains
(+ 0 more) 840 a.a. *
(+ 0 more) 145 a.a. *
(+ 0 more) 147 a.a. *
(+ 8 more) 372 a.a. *
* Residue conservation analysis
PDB id:
1o1d
Name: Contractile protein
Title: Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
Structure: Skeletal muscle myosin ii. Chain: a, d, g, j, m, p. Skeletal muscle myosin ii regulatory light chain. Chain: b, e, h, k, n, q. Skeletal muscle myosin ii essential light chain. Chain: c, f, i, l, o, r. Skeletal muscle actin. Chain: 0, 1, 2, 3, 4, 5, 7, 8, 9, v, w, x, y, z
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Other_details: organism from which the myosin for the crystal structure that provided 2mys was obtained. Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Other_details: organism from which the actin that provided the
Biol. unit: 32mer (from PQS)
Authors: L.F.Chen,H.Winkler,M.K.Reedy,M.C.Reedy,K.A.Taylor
Key ref: L.F.Chen et al. (2002). Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle. J Struct Biol, 138, 92-104. PubMed id: 12160705 DOI: 10.1016/S1047-8477(02)00013-8
Date:
18-Nov-02     Release date:   04-Dec-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P13538  (MYSS_CHICK) -  Myosin heavy chain, skeletal muscle, adult from Gallus gallus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1939 a.a.
840 a.a.*
Protein chains
Pfam   ArchSchema ?
P02609  (MYL11_CHICK) -  Myosin regulatory light chain 11 from Gallus gallus
Seq:
Struc: 		168 a.a.
145 a.a.*
Protein chains
Pfam   ArchSchema ?
P02605  (MLE3_CHICK) -  Myosin light chain 3, skeletal muscle isoform from Gallus gallus
Seq:
Struc: 		150 a.a.
147 a.a.*
Protein chains
Pfam   ArchSchema ?
P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle from Oryctolagus cuniculus
Seq:
Struc: 		377 a.a.
372 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 75 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains 0, 1, 2, 3, 4, 5, 7, 8, 9, V, W, X, Y, Z: E.C.3.6.4.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/S1047-8477(02)00013-8 J Struct Biol 138:92-104 (2002)
PubMed id: 12160705  
 
 
Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle.
L.F.Chen, H.Winkler, M.K.Reedy, M.C.Reedy, K.A.Taylor.
 
  ABSTRACT  
 
Electron tomography, correspondence analysis, molecular model building, and real-space refinement provide detailed 3-D structures for in situ myosin crossbridges in the nucleotide-free state (rigor), thought to represent the end of the power stroke. Unaveraged tomograms from a 25-nm longitudinal section of insect flight muscle preserved native structural variation. Recurring crossbridge motifs that repeat every 38.7 nm along the actin filament were extracted from the tomogram and classified by correspondence analysis into 25 class averages, which improved the signal to noise ratio. Models based on the atomic structures of actin and of myosin subfragment 1 were rebuilt to fit 11 class averages. A real-space refinement procedure was applied to quantitatively fit the reconstructions and to minimize steric clashes between domains introduced during the fitting. These combined procedures show that no single myosin head structure can fit all the in situ crossbridges. The validity of the approach is supported by agreement of these atomic models with fluorescent probe data from vertebrate muscle as well as with data from regulatory light chain crosslinking between heads of smooth muscle heavy meromyosin when bound to actin.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21536289 S.Matsushita, Y.Inoue, M.Hojo, M.Sokabe, and T.Adachi (2011).
Effect of tensile force on the mechanical behavior of actin filaments.
  J Biomech, 44, 1776-1781.  
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.  
20385845 V.Nucciotti, C.Stringari, L.Sacconi, F.Vanzi, L.Fusi, M.Linari, G.Piazzesi, V.Lombardi, and F.S.Pavone (2010).
Probing myosin structural conformation in vivo by second-harmonic generation microscopy.
  Proc Natl Acad Sci U S A, 107, 7763-7768.  
19698791 S.Wu, J.Liu, M.C.Reedy, H.Winkler, M.K.Reedy, and K.A.Taylor (2009).
Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle.
  J Struct Biol, 168, 485-502.  
19452133 W.Hwang, and M.J.Lang (2009).
Mechanical design of translocating motor proteins.
  Cell Biochem Biophys, 54, 11-22.  
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.  
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.  
17548820 M.Kovács, K.Thirumurugan, P.J.Knight, and J.R.Sellers (2007).
Load-dependent mechanism of nonmuscle myosin 2.
  Proc Natl Acad Sci U S A, 104, 9994-9999.  
16689634 T.G.Frey, G.A.Perkins, and M.H.Ellisman (2006).
Electron tomography of membrane-bound cellular organelles.
  Annu Rev Biophys Biomol Struct, 35, 199-224.  
15705568 M.Kovács, F.Wang, and J.R.Sellers (2005).
Mechanism of action of myosin X, a membrane-associated molecular motor.
  J Biol Chem, 280, 15071-15083.  
15766539 S.Dutta, and H.M.Berman (2005).
Large macromolecular complexes in the Protein Data Bank: a status report.
  Structure, 13, 381-388.  
15952904 V.Lucić, F.Förster, and W.Baumeister (2005).
Structural studies by electron tomography: from cells to molecules.
  Annu Rev Biochem, 74, 833-865.  
15111417 B.A.Baumann, H.Liang, K.Sale, B.D.Hambly, and P.G.Fajer (2004).
Myosin regulatory domain orientation in skeletal muscle fibers: application of novel electron paramagnetic resonance spectral decomposition and molecular modeling methods.
  Biophys J, 86, 3030-3041.  
15111415 R.T.Tregear, M.C.Reedy, Y.E.Goldman, K.A.Taylor, H.Winkler, C.Franzini-Armstrong, H.Sasaki, C.Lucaveche, and M.K.Reedy (2004).
Cross-bridge number, position, and angle in target zones of cryofixed isometrically active insect flight muscle.
  Biophys J, 86, 3009-3019.  
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.  
12885655 M.Reconditi, N.Koubassova, M.Linari, I.Dobbie, T.Narayanan, O.Diat, G.Piazzesi, V.Lombardi, and M.Irving (2003).
The conformation of myosin head domains in rigor muscle determined by X-ray interference.
  Biophys J, 85, 1098-1110.  
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.

 

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