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| | <StructureSection load='1ziq' size='340' side='right'caption='[[1ziq]], [[Resolution|resolution]] 1.72Å' scene=''> | | <StructureSection load='1ziq' size='340' side='right'caption='[[1ziq]], [[Resolution|resolution]] 1.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ziq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZIQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ziq]] 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=1ZIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZIQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></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]] 1.72Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a5d|1a5d]], [[1zgt|1zgt]], [[1zie|1zie]], [[1zir|1zir]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></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=1ziq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ziq OCA], [http://pdbe.org/1ziq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ziq RCSB], [http://www.ebi.ac.uk/pdbsum/1ziq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ziq ProSAT]</span></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=1ziq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ziq OCA], [https://pdbe.org/1ziq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ziq RCSB], [https://www.ebi.ac.uk/pdbsum/1ziq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ziq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CRGE_RAT CRGE_RAT]] Crystallins are the dominant structural components of the vertebrate eye lens. | + | [https://www.uniprot.org/uniprot/CRGE_RAT CRGE_RAT] 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Artero, J B]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Hartlein, M]] | + | [[Category: Artero JB]] |
| - | [[Category: McSweeney, S]] | + | [[Category: Hartlein M]] |
| - | [[Category: Timmins, P]] | + | [[Category: McSweeney S]] |
| - | [[Category: Greek key motif]]
| + | [[Category: Timmins P]] |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
CRGE_RAT Crystallins are the dominant structural components of the vertebrate eye lens.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Artero JB, Hartlein M, McSweeney S, Timmins P. A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1541-9. Epub 2005, Oct 19. PMID:16239733 doi:http://dx.doi.org/10.1107/S0907444905028532
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