5b84: Difference between revisions
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<StructureSection load='5b84' size='340' side='right' caption='[[5b84]], [[Resolution|resolution]] 1.61Å' scene=''> | <StructureSection load='5b84' size='340' side='right' caption='[[5b84]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5b84]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B84 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5b84]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B84 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> | </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">[[5b85|5b85]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b85|5b85]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYCD])</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=5b84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b84 OCA], [http://pdbe.org/5b84 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b84 RCSB], [http://www.ebi.ac.uk/pdbsum/5b84 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b84 ProSAT]</span></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=5b84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b84 OCA], [http://pdbe.org/5b84 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b84 RCSB], [http://www.ebi.ac.uk/pdbsum/5b84 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b84 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Phycd]] | |||
[[Category: Yuan, H]] | [[Category: Yuan, H]] | ||
[[Category: Oxygen storage]] | [[Category: Oxygen storage]] | ||
Revision as of 15:23, 6 November 2017
X-ray crystal structure of met I107Y sperm whale myoglobinX-ray crystal structure of met I107Y sperm whale myoglobin
Structural highlights
Function[MYG_PHYCD] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedA hydrogen-bond (H-bond) network, specifically a Tyr-associated H-bond network, plays key roles in regulating the structure and function of proteins, as exemplified by abundant heme proteins in nature. To explore an approach for fine-tuning the structure and function of artificial heme proteins, we herein used myoglobin (Mb) as a model protein and introduced a Tyr residue in the secondary sphere of the heme active site at two different positions (107 and 138). We performed X-ray crystallography, UV-Vis spectroscopy, stopped-flow kinetics, and electron paramagnetic resonance (EPR) studies for the two single mutants, I107Y Mb and F138Y Mb, and compared to that of wild-type Mb under the same conditions. The results showed that both Tyr107 and Tyr138 form a distinct H-bond network involving water molecules and neighboring residues, which fine-tunes ligand binding to the heme iron and enhances the protein stability, respectively. Moreover, the Tyr107-associated H-bond network was shown to fine-tune both H2O2 binding and activation. With two cases demonstrated for Mb, this study suggests that the Tyr-associated H-bond network has distinct roles in regulating the protein structure, properties and functions, depending on its location in the protein scaffold. Therefore, it is possible to design a Tyr-associated H-bond network in general to create other artificial heme proteins with improved properties and functions. Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin.,Liao F, Yuan H, Du KJ, You Y, Gao SQ, Wen GB, Lin YW, Tan X Mol Biosyst. 2016 Aug 1. PMID:27476534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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