This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5b7c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:53, 3 April 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='5b7c' size='340' side='right'caption='[[5b7c]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='5b7c' size='340' side='right'caption='[[5b7c]], [[Resolution|resolution]] 2.35&Aring;' 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</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='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>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A0A1C7D1H4_OCTVU A0A1C7D1H4_OCTVU]
-
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<ref>PMID:27499004</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, 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>
-
[[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]]
+

Current revision

Crystal structure of octopus S-crystallin Q108F mutant in complex with glutathione

PDB ID 5b7c

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5b7c"
Personal tools