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1zgt

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[[Image:1zgt.gif|left|200px]]
 
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==Structure of hydrogenated rat gamma E crystallin in H2O==
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The line below this paragraph, containing "STRUCTURE_1zgt", creates the "Structure Box" on the page.
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<StructureSection load='1zgt' size='340' side='right'caption='[[1zgt]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1zgt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZGT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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{{STRUCTURE_1zgt| PDB=1zgt | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zgt OCA], [https://pdbe.org/1zgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zgt RCSB], [https://www.ebi.ac.uk/pdbsum/1zgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zgt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRGE_RAT CRGE_RAT] Crystallins are the dominant structural components of the vertebrate eye lens.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/1zgt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1zgt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values.
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'''Structure of hydrogenated rat gamma E crystallin in H2O'''
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A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.,Artero JB, Hartlein M, McSweeney S, Timmins P Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1541-9. Epub 2005, Oct 19. PMID:16239733<ref>PMID:16239733</ref>
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==Overview==
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Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1ZGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGT OCA].
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</div>
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<div class="pdbe-citations 1zgt" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O., Artero JB, Hartlein M, McSweeney S, Timmins P, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1541-9. Epub 2005, Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16239733 16239733]
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*[[Crystallin 3D structures|Crystallin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Artero JB]]
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[[Category: Artero, J B.]]
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[[Category: Hartlein M]]
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[[Category: Hartlein, M.]]
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[[Category: McSweeney S]]
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[[Category: McSweeney, S.]]
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[[Category: Timmins P]]
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[[Category: Timmins, P.]]
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[[Category: 4 greek key motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:36:28 2008''
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Current revision

Structure of hydrogenated rat gamma E crystallin in H2O

PDB ID 1zgt

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