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4gcr
From Proteopedia
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| - | [[Image:4gcr.jpg|left|200px]] | ||
| - | + | ==STRUCTURE OF THE BOVINE EYE LENS PROTEIN GAMMA-B (GAMMA-II)-CRYSTALLIN AT 1.47 ANGSTROMS== | |
| - | + | <StructureSection load='4gcr' size='340' side='right'caption='[[4gcr]], [[Resolution|resolution]] 1.47Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4gcr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gcr 1gcr]. The July 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Crystallins'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_7 10.2210/rcsb_pdb/mom_2010_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GCR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GCR FirstGlance]. <br> | |
| - | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gcr OCA], [http://pdbe.org/4gcr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gcr RCSB], [http://www.ebi.ac.uk/pdbsum/4gcr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gcr ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [[http://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN]] Crystallins are the dominant structural components of the vertebrate eye lens. | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | == | + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gc/4gcr_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=4gcr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | Structure of the bovine eye lens protein gammaB(gammaII)-crystallin at 1.47 A.,Najmudin S, Nalini V, Driessen HP, Slingsby C, Blundell TL, Moss DS, Lindley PF Acta Crystallogr D Biol Crystallogr. 1993 Mar 1;49(Pt 2):223-33. PMID:15299528<ref>PMID:15299528</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 4gcr" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Blundell, T L | + | <references/> |
| - | [[Category: Driessen, H P.C | + | __TOC__ |
| - | [[Category: Lindley, P | + | </StructureSection> |
| - | [[Category: Moss, D S | + | [[Category: Bovin]] |
| - | [[Category: Najmudin, S | + | [[Category: Crystallins]] |
| - | [[Category: Nalini, V | + | [[Category: Large Structures]] |
| - | [[Category: Slingsby, C | + | [[Category: RCSB PDB Molecule of the Month]] |
| + | [[Category: Blundell, T L]] | ||
| + | [[Category: Driessen, H P.C]] | ||
| + | [[Category: Lindley, P]] | ||
| + | [[Category: Moss, D S]] | ||
| + | [[Category: Najmudin, S]] | ||
| + | [[Category: Nalini, V]] | ||
| + | [[Category: Slingsby, C]] | ||
[[Category: Eye lens protein]] | [[Category: Eye lens protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:30 2008'' | ||
Current revision
STRUCTURE OF THE BOVINE EYE LENS PROTEIN GAMMA-B (GAMMA-II)-CRYSTALLIN AT 1.47 ANGSTROMS
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