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PDBsum entry 1g1c
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Structural protein PDB id
1g1c

 

 

 

 

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Contents
Protein chains
98 a.a. *
Waters ×198
* Residue conservation analysis
PDB id:
1g1c
Name: Structural protein
Title: I1 domain from titin
Structure: Immunoglobulin-like domain i1 from titin. Chain: a, b. Fragment: most n-terminal ig domain, residues 2027-2125. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: heart. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.10Å     R-factor:   0.202     R-free:   0.248
Authors: O.Mayans,J.Wuerges,M.Gautel,M.Wilmanns
Key ref:
O.Mayans et al. (2001). Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. Structure, 9, 331-340. PubMed id: 11525170 DOI: 10.1016/S0969-2126(01)00591-3
Date:
11-Oct-00     Release date:   12-Oct-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8WZ42  (TITIN_HUMAN) -  Titin from Homo sapiens
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Struc: 		34350 a.a.
98 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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: 10.1016/S0969-2126(01)00591-3 Structure 9:331-340 (2001)
PubMed id: 11525170  
 
 
Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.
O.Mayans, J.Wuerges, S.Canela, M.Gautel, M.Wilmanns.
 
  ABSTRACT  
 
BACKGROUND: The giant muscle protein titin contributes to the filament system in skeletal and cardiac muscle cells by connecting the Z disk and the central M line of the sarcomere. One of the physiological functions of titin is to act as a passive spring in the sarcomere, which is achieved by the elastic properties of its central I band region. Titin contains about 300 domains of which more than half are folded as immunoglobulin-like (Ig) domains. Ig domain segments of the I band of titin have been extensively used as templates to investigate the molecular basis of protein elasticity. RESULTS: The structure of the Ig domain I1 from the I band of titin has been determined to 2.1 A resolution. It reveals a novel, reversible disulphide bridge, which is neither required for correct folding nor changes the chemical stability of I1, but it is predicted to contribute mechanically to the elastic properties of titin in active sarcomeres. From the 92 Ig domains in the longest isoform of titin, at least 40 domains have a potential for disulphide bridge formation. CONCLUSIONS: We propose a model where the formation of disulphide bridges under oxidative stress conditions could regulate the elasticity of the I band in titin by increasing sarcomeric resistance. In this model, the formation of the disulphide bridge could refrain a possible directed motion of the two beta sheets or other mechanically stable entities of the I1 Ig domain with respect to each other when exposed to mechanical forces.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Overall Structure of the I1 Ig Domain(a) Ribbon representation. b strands of the sheets ABDE and the A'CC'FG are color coded in pink and cyan, respectively. The two loops B-C and F-G, close to the N terminus, are colored in light green and dark green, respectively. The two loops A'-B and E-F, close to the C terminus, are colored in orange and brown, respectively.(b) Same presentation as (a) but tilted. The disulphide bridge connecting residues 37 (b strand C) and 62 (b strand E) is shown in ball-and-stick representation. The 3 tryptophan residues (W39, W54, and W56) surrounding the disulphide bridge are also included.(c) Stereoview of the 2F[o]-F[c] (a[calc]) electron density map of the disulphide bridge region contoured at 1.5 s

 
  The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 331-340) copyright 2001.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21332356 J.Hsin, J.Strümpfer, E.H.Lee, and K.Schulten (2011).
Molecular origin of the hierarchical elasticity of titin: simulation, experiment, and theory.
  Annu Rev Biophys, 40, 187-203.  
19651040 A.Grützner, S.Garcia-Manyes, S.Kötter, C.L.Badilla, J.M.Fernandez, and W.A.Linke (2009).
Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence.
  Biophys J, 97, 825-834.  
  19789381 A.Kontrogianni-Konstantopoulos, M.A.Ackermann, A.L.Bowman, S.V.Yap, and R.J.Bloch (2009).
Muscle giants: molecular scaffolds in sarcomerogenesis.
  Physiol Rev, 89, 1217-1267.  
19466753 C.A.Otey, R.Dixon, C.Stack, and S.M.Goicoechea (2009).
Cytoplasmic Ig-domain proteins: cytoskeletal regulators with a role in human disease.
  Cell Motil Cytoskeleton, 66, 618-634.  
19572737 J.Liang, and J.M.Fernández (2009).
Mechanochemistry: One Bond at a Time.
  ACS Nano, 3, 1628-1645.  
19003986 T.I.Garcia, A.F.Oberhauser, and W.Braun (2009).
Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains.
  Proteins, 75, 706-718.  
18926831 A.Ababou, E.Rostkova, S.Mistry, C.Le Masurier, M.Gautel, and M.Pfuhl (2008).
Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1.
  J Mol Biol, 384, 615-630.
PDB code: 2avg
18223005 E.Eyal, and I.Bahar (2008).
Toward a molecular understanding of the anisotropic response of proteins to external forces: insights from elastic network models.
  Biophys J, 94, 3424-3435.  
19111067 R.R.Thangudu, M.Manoharan, N.Srinivasan, F.Cadet, R.Sowdhamini, and B.Offmann (2008).
Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families.
  BMC Struct Biol, 8, 55.  
18352054 S.Marchetti, F.Sbrana, R.Raccis, L.Lanzi, C.M.Gambi, M.Vassalli, B.Tiribilli, A.Pacini, and A.Toscano (2008).
Dynamic light scattering and atomic force microscopy imaging on fragments of beta-connectin from human cardiac muscle.
  Phys Rev E Stat Nonlin Soft Matter Phys, 77, 021910.  
18058125 W.A.Linke, and A.Grützner (2008).
Pulling single molecules of titin by AFM--recent advances and physiological implications.
  Pflugers Arch, 456, 101-115.  
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
17496052 E.H.Lee, J.Hsin, O.Mayans, and K.Schulten (2007).
Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.
  Biophys J, 93, 1719-1735.  
16896432 M.Gao, M.Sotomayor, E.Villa, E.H.Lee, and K.Schulten (2006).
Molecular mechanisms of cellular mechanics.
  Phys Chem Chem Phys, 8, 3692-3706.  
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
15740352 M.Cieplak, A.Pastore, and T.X.Hoang (2005).
Mechanical properties of the domains of titin in a Go-like model.
  J Chem Phys, 122, 54906.  
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.  
15322090 L.Tskhovrebova, and J.Trinick (2004).
Properties of titin immunoglobulin and fibronectin-3 domains.
  J Biol Chem, 279, 46351-46354.  
15211512 M.Cieplak, T.X.Hoang, and M.O.Robbins (2004).
Thermal effects in stretching of Go-like models of titin and secondary structures.
  Proteins, 56, 285-297.  
14506471 L.Tskhovrebova, and J.Trinick (2003).
Titin: properties and family relationships.
  Nat Rev Mol Cell Biol, 4, 679-689.  
11746222 L.Janda, J.Damborský, G.A.Rezniczek, and G.Wiche (2001).
Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions.
  Bioessays, 23, 1064-1069.  
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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