1elp: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1elp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELP FirstGlance]. <br>
<table><tr><td colspan='2'>[[1elp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELP FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1elp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elp OCA], [https://pdbe.org/1elp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elp RCSB], [https://www.ebi.ac.uk/pdbsum/1elp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elp ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1elp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elp OCA], [https://pdbe.org/1elp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elp RCSB], [https://www.ebi.ac.uk/pdbsum/1elp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CRGD_BOVIN CRGD_BOVIN]] Crystallins are the dominant structural components of the vertebrate eye lens.  
[https://www.uniprot.org/uniprot/CRGD_BOVIN CRGD_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1elp ConSurf].
</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=1elp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of bovine lens gammaIIIb-crystallin at 2.5 A resolution previously reported was interpreted using a consensus sequence derived from related vertebrate sequences on the assumption that gammaIIIb-crystallin derived from the gammaC-crystallin gene. It has recently been shown that gammaIIIb is a product of the bovine gammaD gene. The structure of gammaIIIb has now been refined with the bovine gammaD sequence using new 1.95 A resolution synchrotron data. The crystallographic R factor was 20.4% for all 33 104 reflection data between 8.0 and 1.95 A measured at 277(1) K. The electron density fully supported the assignment of the gammaD sequence to gammaIIIb. The crystal belongs to space group P2(1)2(1)2(1) with two molecules of molecular mass 20 749 Da in the asymmetric unit in which 219 water molecules were located. The two-domain four-Greek-key motif highly symmetrical protein is very similar in structure to gammaB-crystallin (81% sequence identity). There is a single amino-acid deletion in gammaD in the linker region connecting the two domains. The intermolecular oganization in the crystal lattice is quite different from gammaB as a result of key mutations involving surface residues Leu51, Ile103 and His155. These point mutations will contribute to the intermolecular behaviour of the gamma-crystallins in the eye lens, where they are major components of the densely packed, high refractive index regions of the lens.
Structure of bovine eye lens gammaD (gammaIIIb)-crystallin at 1.95 A.,Chirgadze YN, Driessen HP, Wright G, Slingsby C, Hay RE, Lindley PF Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):712-21. PMID:15299634<ref>PMID:15299634</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1elp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Crystallin 3D structures|Crystallin 3D structures]]
*[[Crystallin 3D structures|Crystallin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chirgadze, Yu N]]
[[Category: Chirgadze YuN]]
[[Category: Driessen, H P.C]]
[[Category: Driessen HPC]]
[[Category: Hay, R E]]
[[Category: Hay RE]]
[[Category: Lindley, P F]]
[[Category: Lindley PF]]
[[Category: Slingsby, C]]
[[Category: Slingsby C]]
[[Category: Wright, G]]
[[Category: Wright G]]
[[Category: Eye lens protein]]

Latest revision as of 07:04, 7 February 2024

GAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION

1elp, resolution 1.95Å

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