|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4tyx' size='340' side='right'caption='[[4tyx]], [[Resolution|resolution]] 1.64Å' scene=''> | | <StructureSection load='4tyx' size='340' side='right'caption='[[4tyx]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tyx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phymc Phymc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TYX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tyx]] 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=4TYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TYX 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" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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 PHYMC])</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=4tyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyx OCA], [https://pdbe.org/4tyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tyx RCSB], [https://www.ebi.ac.uk/pdbsum/4tyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tyx 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=4tyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyx OCA], [http://pdbe.org/4tyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tyx RCSB], [http://www.ebi.ac.uk/pdbsum/4tyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tyx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 26: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phymc]] | + | [[Category: Physeter catodon]] |
| - | [[Category: Bhagi-Damodaran, A]] | + | [[Category: Bhagi-Damodaran A]] |
| - | [[Category: Lu, Y]] | + | [[Category: Lu Y]] |
| - | [[Category: Petrik, I D]] | + | [[Category: Petrik ID]] |
| - | [[Category: Robinson, H]] | + | [[Category: Robinson H]] |
| - | [[Category: Artificial]]
| + | |
| - | [[Category: Engineered]]
| + | |
| - | [[Category: Globin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Publication Abstract from PubMed
Cytochrome c Oxidase (CcO) is known to catalyze the reduction of O2 to H2O efficiently with a much lower overpotential than almost all other O2 reduction catalysts. However, the methods by which the enzyme fine-tunes the reduction potential (E degrees ) of its active site and its influence on the O2 reduction activity are not well understood. In this work, we report systematic tuning of the heme E degrees in a functional model of CcO in myoglobin containing three histidines and one tyrosine in the distal pocket of heme. By removing H-bonding interactions between Ser92, and the proximal His ligand through Ser92Ala mutation, we have increased the heme E degrees from 95 +/- 2 mV to 123 +/- 3 mV . Additionally, replacing the native heme b in the protein with heme a analogs, diacetyl, monoformyl and diformyl heme, resulted in an E degrees value of 175 +/- 5 mV, 210 +/- 6 mV and 320 +/- 10 mV, respectively. Interestingly, a strong enhancement of the O2 reduction activity was observed with increasing heme E degrees . The methods of tuning the heme E degrees through a combination of secondary sphere mutations and heme substitutions can be applied to tune E degrees of other heme proteins, allowing for comprehensive investigations of the relationship between E degrees and enzymatic activity.
Systematic Tuning of Heme Redox Potentials and its Effects on O Reduction Rates in a Designed Oxidase in Myoglobin.,Bhagi-Damodaran A, Petrik ID, Marshall NM, Robinson H, Lu Y J Am Chem Soc. 2014 Jul 30. PMID:25076049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bhagi-Damodaran A, Petrik ID, Marshall NM, Robinson H, Lu Y. Systematic Tuning of Heme Redox Potentials and its Effects on O Reduction Rates in a Designed Oxidase in Myoglobin. J Am Chem Soc. 2014 Jul 30. PMID:25076049 doi:http://dx.doi.org/10.1021/ja5054863
|
