|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2g10' size='340' side='right'caption='[[2g10]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2g10' size='340' side='right'caption='[[2g10]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g10]] 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=2G10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G10 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g10]] 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=2G10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G10 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2g0v|2g0v]], [[2g0x|2g0x]], [[2g0z|2g0z]], [[2g11|2g11]], [[2g12|2g12]], [[2g14|2g14]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</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=2g10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g10 OCA], [https://pdbe.org/2g10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g10 RCSB], [https://www.ebi.ac.uk/pdbsum/2g10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g10 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=2g10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g10 OCA], [https://pdbe.org/2g10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g10 RCSB], [https://www.ebi.ac.uk/pdbsum/2g10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g10 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]] |
| Line 38: |
Line 37: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phymc]] | + | [[Category: Physeter catodon]] |
| - | [[Category: Anfinrud, P A]] | + | [[Category: Anfinrud PA]] |
| - | [[Category: Aranda, R]] | + | [[Category: Aranda R]] |
| - | [[Category: Levin, E J]] | + | [[Category: Levin EJ]] |
| - | [[Category: Phillips, G N]] | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Schotte, F]] | + | [[Category: Schotte F]] |
| - | [[Category: Difference refinement]]
| + | |
| - | [[Category: Intermediate state]]
| + | |
| - | [[Category: Myoglobin]]
| + | |
| - | [[Category: Structure-function relationship]]
| + | |
| - | [[Category: Time-resolved crystallography]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| 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
Picosecond time-resolved crystallography was used to follow the dissociation of carbon monoxide from the heme pocket of a mutant sperm whale myoglobin and the resultant conformational changes. Electron-density maps have previously been created at various time points and used to describe amino-acid side-chain and carbon monoxide movements. In this work, difference refinement was employed to generate atomic coordinates at each time point in order to create a more explicit quantitative representation of the photo-dissociation process. After photolysis the carbon monoxide moves to a docking site, causing rearrangements in the heme-pocket residues, the coordinate changes of which can be plotted as a function of time. These include rotations of the heme-pocket phenylalanine concomitant with movement of the distal histidine toward the solvent, potentially allowing carbon monoxide movement in and out of the protein and proximal displacement of the heme iron. The degree of relaxation toward the intermediate and deoxy states was probed by analysis of the coordinate movements in the time-resolved models, revealing a non-linear progression toward the unbound state with coordinate movements that begin in the heme-pocket area and then propagate throughout the rest of the protein.
Time-dependent atomic coordinates for the dissociation of carbon monoxide from myoglobin.,Aranda R 4th, Levin EJ, Schotte F, Anfinrud PA, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):776-83. Epub 2006, Jun 20. PMID:16790933[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Aranda R 4th, Levin EJ, Schotte F, Anfinrud PA, Phillips GN Jr. Time-dependent atomic coordinates for the dissociation of carbon monoxide from myoglobin. Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):776-83. Epub 2006, Jun 20. PMID:16790933 doi:10.1107/S0907444906017318
|
