5zeo
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==X-ray structure of sperm whale V21C/V66C/F46S myoglobin mutant with an intramolecular disulfide bond== | |
+ | <StructureSection load='5zeo' size='340' side='right' caption='[[5zeo]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5zeo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZEO FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=5zeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zeo OCA], [http://pdbe.org/5zeo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zeo RCSB], [http://www.ebi.ac.uk/pdbsum/5zeo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zeo ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | A de novo designed intramolecular disulfide bond in myoglobin, resembling that in cytoglobin without structural evidence, was confirmed by an X-ray structure for the first time and was demonstrated to regulate both the structure and function of this protein, which fulfills the design of an artificial dehaloperoxidase, with an activity exceeding that of a native enzyme. | ||
- | + | Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin.,Yin LL, Yuan H, Du KJ, He B, Gao SQ, Wen GB, Tan X, Lin YW Chem Commun (Camb). 2018 Apr 24;54(34):4356-4359. doi: 10.1039/c8cc01646a. PMID:29645029<ref>PMID:29645029</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
+ | <div class="pdbe-citations 5zeo" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Yuan, H]] | [[Category: Yuan, H]] | ||
+ | [[Category: Myoglobin]] | ||
+ | [[Category: Oxygen transport]] | ||
+ | [[Category: Sperm whale]] |
Revision as of 06:14, 9 May 2018
X-ray structure of sperm whale V21C/V66C/F46S myoglobin mutant with an intramolecular disulfide bond
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