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| | <StructureSection load='2ohb' size='340' side='right'caption='[[2ohb]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2ohb' size='340' side='right'caption='[[2ohb]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ohb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phymc Phymc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OHB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ohb]] 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=2OHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OHB FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oh8|2oh8]], [[2oh9|2oh9]], [[2oha|2oha]]</div></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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([https://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=2ohb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ohb OCA], [https://pdbe.org/2ohb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ohb RCSB], [https://www.ebi.ac.uk/pdbsum/2ohb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ohb ProSAT]</span></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=2ohb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ohb OCA], [https://pdbe.org/2ohb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ohb RCSB], [https://www.ebi.ac.uk/pdbsum/2ohb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ohb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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.
| + | [https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phymc]] | + | [[Category: Physeter catodon]] |
| - | [[Category: Olson, J S]] | + | [[Category: Olson JS]] |
| - | [[Category: Phillips, G N]] | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Schweers, R L]] | + | [[Category: Schweers RL]] |
| - | [[Category: Soman, J]] | + | [[Category: Soman J]] |
| - | [[Category: Ligand entry and exit pathway]]
| + | |
| - | [[Category: Myoglobin]]
| + | |
| - | [[Category: Oxygen storage-transport complex]]
| + | |
| Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The pathways for ligand entry and exit in myoglobin have now been well established by a wide variety of experimental results, including pico- to nano- to microsecond transient absorbance measurements and time-resolved X-ray crystallographic measurements. Trp insertions have been used to block, one at a time, the three major cavities occupied by photodissociated ligands. In this work, we review the effects of the L29(B10)W mutation, which places a large indole ring in the initial 'docking site' for photodissociated ligands. Then, the effects of blocking the Xe4 site with I28W, V68W, and I107W mutations and the Xe1 cavity with L89W, L104W, and F138W mutations are described. The structures of four of these mutants are shown for the first time (Trp28, Trp68, Trp107, and Trp 138 sperm whale metMb). All available results support a 'side path' mechanism in which ligands move into and out of myoglobin by outward rotation of the HisE7 side chain, but after entry can migrate into internal cavities, including the distal Xe4 and proximal Xe1 binding sites. The distal cavities act like the pocket of a baseball glove, catching the ligand and holding it long enough for the histidine gate to close and facilitate internal coordination with the heme iron atom. The physiological role of the proximal Xe1 site is less clear because changes in the size of this cavity have minimal effects on overall O(2) binding parameters.
Ligand pathways in myoglobin: a review of Trp cavity mutations.,Olson JS, Soman J, Phillips GN Jr IUBMB Life. 2007 Aug-Sep;59(8-9):552-62. PMID:17701550[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Olson JS, Soman J, Phillips GN Jr. Ligand pathways in myoglobin: a review of Trp cavity mutations. IUBMB Life. 2007 Aug-Sep;59(8-9):552-62. PMID:17701550
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