4qau: Difference between revisions
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''' | ==Crystal structure of F43Y mutant of sperm whale myoglobin== | ||
<StructureSection load='4qau' size='340' side='right' caption='[[4qau]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qau]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QAU 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4it8|4it8]]</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=4qau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qau OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qau RCSB], [http://www.ebi.ac.uk/pdbsum/4qau PDBsum]</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 == | |||
Heme post-translational modification plays a key role in tuning the structure and function of heme proteins. We herein report a novel tyrosine-heme covalent CO bond in an artificially produced sperm whale myoglobin (Mb) mutant, F43Y Mb, which formed spontaneously in vivo between the Tyr43 hydroxy group and the heme 4-vinyl group. This highlights the diverse chemistry of heme post-translational modifications, and lays groundwork for further investigation of the structural and functional diversity of covalently-bound heme proteins. | |||
A Novel Tyrosine-Heme CO Covalent Linkage in F43Y Myoglobin: A New Post-translational Modification of Heme Proteins.,Yan DJ, Li W, Xiang Y, Wen GB, Lin YW, Tan X Chembiochem. 2015 Jan 2;16(1):47-50. doi: 10.1002/cbic.201402504. Epub 2014 Nov, 12. PMID:25392956<ref>PMID:25392956</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Li, W]] | [[Category: Li, W]] | ||
[[Category: Lin, Y]] | [[Category: Lin, Y]] | ||
[[Category: Tan, X]] | |||
[[Category: Alpha helix boundle]] | |||
[[Category: F43y mutant]] | |||
[[Category: Oxygen transport]] | |||
Revision as of 16:46, 21 January 2015
Crystal structure of F43Y mutant of sperm whale myoglobin
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