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Eye lens protein PDB id
4gcr
Jmol
Contents
Protein chain
174 a.a. *
Waters ×230
* Residue conservation analysis
PDB id:
4gcr
Name: Eye lens protein
Title: Structure of the bovine eye lens protein gamma-b (gamma-ii)- crystallin at 1.47 angstroms
Structure: Gamma-b crystallin. Chain: a. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913
Resolution:
1.47Å     R-factor:   0.181    
Authors: C.Slingsby,S.Najmudin,V.Nalini,H.P.C.Driessen,T.L.Blundell, D.S.Moss,P.Lindley
Key ref:
S.Najmudin et al. (1993). Structure of the bovine eye lens protein gammaB(gammaII)-crystallin at 1.47 A. Acta Crystallogr D Biol Crystallogr, 49, 223-233. PubMed id: 15299528 DOI: 10.1107/S0907444992007601
Date:
02-Apr-92     Release date:   31-Oct-93    
Supersedes: 1gcr
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02526  (CRGB_BOVIN) -  Gamma-crystallin B
Seq:
Struc:
175 a.a.
174 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     eye development   4 terms 
  Biochemical function     structural constituent of eye lens     1 term  

 

 
DOI no: 10.1107/S0907444992007601 Acta Crystallogr D Biol Crystallogr 49:223-233 (1993)
PubMed id: 15299528  
 
 
Structure of the bovine eye lens protein gammaB(gammaII)-crystallin at 1.47 A.
S.Najmudin, V.Nalini, H.P.Driessen, C.Slingsby, T.L.Blundell, D.S.Moss, P.F.Lindley.
 
  ABSTRACT  
 
The molecular structure of calf gammaB-crystallin (previously called gammaII), a lens-specific protein, has been refined to a crystallographic R factor of 18.1% for all reflection data, between 8.0 and 1.47 A, 25 959 hkl measured at 293 (1) K. 230 water molecules have been defined by difference Fourier techniques and included in a restrained least-squares refinement. Difference Fourier maps clearly indicated the presence of multiple sites for the sulfur atoms of Cys 18 and Cys 22 which were therefore given coupled second-site occupancies during the refinement. The sulfur atom in the major position of Cys 22 is in the reduced state. Either of the Cys 18 sites can form a high-energy disulfide bridge with the minor position of Cys 22. The position of the carboxy terminus and many other surface side chains have been further defined including the RGD signal peptide. The hydration of the backbone and the interdomain region has been analysed. 27 water molecules make extensive contacts to a single protein molecule and thus contribute to its stability.
 
  Selected figure(s)  
 
Figure 7.
Fig. 7. A stereoview of hydrogen-bonding pattern maintaining the conformation of the RGD sequence which is on the surface of the molecule. The Asp 61 forms an intramolecular ion pair with Arg 36. The sheet structure is extended by a network of waer molecules.
Figure 8.
Fig. 8. A stereo picture of the water network shielding the exposed ydrophobic side chain of Pro 82. Note water molecules 300 and 365 are too close (i.95 A) and are probably the same fluctuating molecule. The electron density is contoured at 0.6 .m.s.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1993, 49, 223-233) copyright 1993.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19548648 K.Srivastava, R.Gupta, J.M.Chaves, and O.P.Srivastava (2009).
Truncated human betaB1-crystallin shows altered structural properties and interaction with human betaA3-crystallin.
  Biochemistry, 48, 7179-7189.  
15908249 P.Garcia-Barreno, M.C.Guisasola, and A.Suarez (2005).
Fluorescent and compositional changes in crystallin supramolecular structures in pig lens during development.
  Comp Biochem Physiol B Biochem Mol Biol, 141, 179-185.  
15345525 I.Navizet, F.Cailliez, and R.Lavery (2004).
Probing protein mechanics: residue-level properties and their use in defining domains.
  Biophys J, 87, 1426-1435.  
12084052 G.D'Alessio (2002).
The evolution of monomeric and oligomeric betagamma-type crystallins. Facts and hypotheses.
  Eur J Biochem, 269, 3122-3130.  
10688888 A.Pande, J.Pande, N.Asherie, A.Lomakin, O.Ogun, J.A.King, N.H.Lubsen, D.Walton, and G.B.Benedek (2000).
Molecular basis of a progressive juvenile-onset hereditary cataract.
  Proc Natl Acad Sci U S A, 97, 1993-1998.  
10400668 N.Li, M.Erman, W.Pangborn, W.L.Duax, C.M.Park, J.Bruenn, and D.Ghosh (1999).
Structure of Ustilago maydis killer toxin KP6 alpha-subunit. A multimeric assembly with a central pore.
  J Biol Chem, 274, 20425-20431.
PDB code: 1kp6
  9541393 S.Palme, R.Jaenicke, and C.Slingsby (1998).
X-ray structures of three interface mutants of gammaB-crystallin from bovine eye lens.
  Protein Sci, 7, 611-618.  
  9232654 S.Palme, C.Slingsby, and R.Jaenicke (1997).
Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens.
  Protein Sci, 6, 1529-1536.  
7862635 J.Pande, A.Lomakin, B.Fine, O.Ogun, I.Sokolinski, and G.Benedek (1995).
Oxidation of gamma II-crystallin solutions yields dimers with a high phase separation temperature.
  Proc Natl Acad Sci U S A, 92, 1067-1071.  
7559623 T.Zhao, and F.A.Bettelheim (1995).
Enthalpy and entropy of hydration of bovine crystallins.
  J Biol Chem, 270, 24961-24964.  
  7849599 S.Zarina, C.Slingsby, R.Jaenicke, Z.H.Zaidi, H.Driessen, and N.Srinivasan (1994).
Three-dimensional model and quaternary structure of the human eye lens protein gamma S-crystallin based on beta- and gamma-crystallin X-ray coordinates and ultracentrifugation.
  Protein Sci, 3, 1840-1846.  
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.