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4qau
From Proteopedia
(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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