5b7c
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5b7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Octopus_vulgaris Octopus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B7C FirstGlance]. <br> | <table><tr><td colspan='2'>[[5b7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Octopus_vulgaris Octopus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B7C FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.35Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5b7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b7c OCA], [https://pdbe.org/5b7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b7c RCSB], [https://www.ebi.ac.uk/pdbsum/5b7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b7c 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=5b7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b7c OCA], [https://pdbe.org/5b7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b7c RCSB], [https://www.ebi.ac.uk/pdbsum/5b7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b7c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A1C7D1H4_OCTVU A0A1C7D1H4_OCTVU] | [https://www.uniprot.org/uniprot/A0A1C7D1H4_OCTVU A0A1C7D1H4_OCTVU] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Crystallins are found widely in animal lenses and have important functions due to their refractive properties. In the coleoid cephalopods, a lens with a graded refractive index provides good vision and is required for survival. Cephalopod S-crystallin is thought to have evolved from glutathione S-transferase (GST) with various homologs differentially expressed in the lens. However, there is no direct structural information that helps to delineate the mechanisms by which S-crystallin could have evolved. Here we report the structural and biochemical characterization of novel S-crystallin-glutathione complex. The 2.35-A crystal structure of a S-crystallin mutant from Octopus vulgaris reveals an active-site architecture that is different from that of GST. S-crystallin has a preference for glutathione binding, although almost lost its GST enzymatic activity. We've also identified four historical mutations that are able to produce a "GST-like" S-crystallin that has regained activity. This protein recapitulates the evolution of S-crystallin from GST. Protein stability studies suggest that S-crystallin is stabilized by glutathione binding to prevent its aggregation; this contrasts with GST-sigma, which do not possess this protection. We suggest that a tradeoff between enzyme activity and the stability of the lens protein might have been one of the major driving force behind lens evolution. | ||
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| - | Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive Protein.,Tan WH, Cheng SC, Liu YT, Wu CG, Lin MH, Chen CC, Lin CH, Chou CY Sci Rep. 2016 Aug 8;6:31176. doi: 10.1038/srep31176. PMID:27499004<ref>PMID:27499004</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5b7c" 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> | ||
Current revision
Crystal structure of octopus S-crystallin Q108F mutant in complex with glutathione
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