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| | <StructureSection load='5b7c' size='340' side='right'caption='[[5b7c]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5b7c' size='340' side='right'caption='[[5b7c]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b7c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_octopus Common octopus]. 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 [http://oca.weizmann.ac.il/oca-docs/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"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5b7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b7c OCA], [http://pdbe.org/5b7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b7c RCSB], [http://www.ebi.ac.uk/pdbsum/5b7c PDBsum], [http://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 == |
| | + | [https://www.uniprot.org/uniprot/A0A1C7D1H4_OCTVU A0A1C7D1H4_OCTVU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Common octopus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chou, C Y]] | + | [[Category: Octopus vulgaris]] |
| - | [[Category: Tan, W H]] | + | [[Category: Chou C-Y]] |
| - | [[Category: Wu, C G]] | + | [[Category: Tan W-H]] |
| - | [[Category: Lens-refractive protein]]
| + | [[Category: Wu C-G]] |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
A0A1C7D1H4_OCTVU
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tan WH, Cheng SC, Liu YT, Wu CG, Lin MH, Chen CC, Lin CH, Chou CY. Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive Protein. Sci Rep. 2016 Aug 8;6:31176. doi: 10.1038/srep31176. PMID:27499004 doi:http://dx.doi.org/10.1038/srep31176
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