4qau: Difference between revisions

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Bots, Bureaucrats, journal, Administrators
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'''Unreleased structure'''


The entry 4qau is ON HOLD  until Paper Publication
==Crystal structure of F43Y mutant of sperm whale myoglobin==
<StructureSection load='4qau' size='340' side='right'caption='[[4qau]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qau]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QAU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.597&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4qau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qau OCA], [https://pdbe.org/4qau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qau RCSB], [https://www.ebi.ac.uk/pdbsum/4qau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qau ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] 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.


Authors: Lin, Y., Tan, X., Li, W.
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>


Description: Crystal structure of F43Y mutant of sperm whale myoglobin
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qau" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Li W]]
[[Category: Lin Y]]
[[Category: Tan X]]
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