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PDBsum entry 1wiu
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Muscle protein PDB id
1wiu

 

 

 

 

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Contents
Protein chain
93 a.a. *
* Residue conservation analysis
PDB id:
1wiu
Name: Muscle protein
Title: Twitchin immunoglobulin superfamily domain (igsf module) (ig 18'), nmr, 30 structures
Structure: Twitchin 18th igsf module. Chain: a. Engineered: yes
Source: Caenorhabditis elegans. Organism_taxid: 6239. Organ: body wall muscle. Tissue: muscle a-band. Cell: muscle cell. Gene: unc-22. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 30 models
Authors: S.Fong,M.Bycroft
Key ref:
S.Fong et al. (1996). Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol, 264, 624-639. PubMed id: 8969309 DOI: 10.1006/jmbi.1996.0665
Date:
23-Jun-96     Release date:   23-Dec-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q23551  (UNC22_CAEEL) -  Twitchin from Caenorhabditis elegans
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Struc: 		7158 a.a.
93 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
 + ATP
 = O-phospho-L-seryl-[protein]
 + ADP
 + H(+)
L-threonyl-[protein]
 + ATP
 = O-phospho-L-threonyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1006/jmbi.1996.0665 J Mol Biol 264:624-639 (1996)
PubMed id: 8969309  
 
 
Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans.
S.Fong, S.J.Hamill, M.Proctor, S.M.Freund, G.M.Benian, C.Chothia, M.Bycroft, J.Clarke.
 
  ABSTRACT  
 
The NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the immunoglobulin superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant.
 
  Selected figure(s)  
 
Figure 8.
Figure 8. Schematic picture of the three-dimensional folding topology of Ig 18' generated from the minimized average structure with the program MolScript (Kraulis, 1991). 		Figure 9.
Figure 9. Stereoview of an overlay of the hydrophobic core residues of telokin, Ig 18', titin M5 and VCAM-d1. The alignment was a structural alignment based on the I set profile shown below. Colours: telokin, purple (backbone shown); Ig 18', cyan; titin M5, red; VCAM-d1, green.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1996, 264, 624-639) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18982379 A.J.Ayme-Southgate, R.J.Southgate, R.A.Philipp, E.E.Sotka, and C.Kramp (2008).
The myofibrillar protein, projectin, is highly conserved across insect evolution except for its PEVK domain.
  J Mol Evol, 67, 653-669.  
17192269 A.Ababou, M.Gautel, and M.Pfuhl (2007).
Dissecting the N-terminal myosin binding site of human cardiac myosin-binding protein C. Structure and myosin binding of domain C2.
  J Biol Chem, 282, 9204-9215.
PDB code: 1pd6
16287100 A.Prasad, H.Zhao, J.M.Rutherford, N.Housley, C.Nichols, and S.Pedigo (2006).
Effect of linker segments on the stability of epithelial cadherin Domain 2.
  Proteins, 62, 111-121.  
16354304 B.A.Manjasetty, F.H.Niesen, C.Scheich, Y.Roske, F.Goetz, J.Behlke, V.Sievert, U.Heinemann, and K.Büssow (2005).
X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1).
  BMC Struct Biol, 5, 21.
PDB code: 1u2h
16341830 M.Marino, D.I.Svergun, L.Kreplak, P.V.Konarev, B.Maco, D.Labeit, and O.Mayans (2005).
Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents.
  J Muscle Res Cell Motil, 26, 355-365.  
16195231 T.Ohashi, and H.P.Erickson (2005).
Domain unfolding plays a role in superfibronectin formation.
  J Biol Chem, 280, 39143-39151.  
11509370 J.G.Head, A.Houmeida, P.J.Knight, A.R.Clarke, J.Trinick, and R.L.Brady (2001).
Stability and folding rates of domains spanning the large A-band super-repeat of titin.
  Biophys J, 81, 1570-1579.  
11566797 M.Gao, H.Lu, and K.Schulten (2001).
Simulated refolding of stretched titin immunoglobulin domains.
  Biophys J, 81, 2268-2277.  
11525170 O.Mayans, J.Wuerges, S.Canela, M.Gautel, and M.Wilmanns (2001).
Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.
  Structure, 9, 331-340.
PDB code: 1g1c
10823892 E.Paci, and M.Karplus (2000).
Unfolding proteins by external forces and temperature: the importance of topology and energetics.
  Proc Natl Acad Sci U S A, 97, 6521-6526.  
10465743 B.Zhang, G.Xu, and J.S.Evans (1999).
A kinetic molecular model of the reversible unfolding and refolding of titin under force extension.
  Biophys J, 77, 1306-1315.  
10339559 D.K.Klimov, and D.Thirumalai (1999).
Stretching single-domain proteins: phase diagram and kinetics of force-induced unfolding.
  Proc Natl Acad Sci U S A, 96, 6166-6170.  
9890894 F.Wang, W.Lu, K.McKeehan, K.Mohamedali, J.L.Gabriel, M.Kan, and W.L.McKeehan (1999).
Common and specific determinants for fibroblast growth factors in the ectodomain of the receptor kinase complex.
  Biochemistry, 38, 160-171.  
10508783 J.Clarke, E.Cota, S.B.Fowler, and S.J.Hamill (1999).
Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway.
  Structure, 7, 1145-1153.  
9889186 M.Bycroft, A.Bateman, J.Clarke, S.J.Hamill, R.Sandford, R.L.Thomas, and C.Chothia (1999).
The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease.
  EMBO J, 18, 297-305.
PDB code: 1b4r
10097099 M.Carrion-Vazquez, A.F.Oberhauser, S.B.Fowler, P.E.Marszalek, S.E.Broedel, J.Clarke, and J.M.Fernandez (1999).
Mechanical and chemical unfolding of a single protein: a comparison.
  Proc Natl Acad Sci U S A, 96, 3694-3699.  
9609701 S.J.Hamill, A.E.Meekhof, and J.Clarke (1998).
The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin.
  Biochemistry, 37, 8071-8079.  
9242926 C.Chothia, and E.Y.Jones (1997).
The molecular structure of cell adhesion molecules.
  Annu Rev Biochem, 66, 823-862.  
9204285 J.Heringa, and W.R.Taylor (1997).
Three-dimensional domain duplication, swapping and stealing.
  Curr Opin Struct Biol, 7, 416-421.  
9148804 M.Rief, M.Gautel, F.Oesterhelt, J.M.Fernandez, and H.E.Gaub (1997).
Reversible unfolding of individual titin immunoglobulin domains by AFM.
  Science, 276, 1109-1112.  
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.

 

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