2g0s: Difference between revisions
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|PDB= 2g0s |SIZE=350|CAPTION= <scene name='initialview01'>2g0s</scene>, resolution 1.90Å | |PDB= 2g0s |SIZE=350|CAPTION= <scene name='initialview01'>2g0s</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <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> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon]) | |GENE= MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0s OCA], [http://www.ebi.ac.uk/pdbsum/2g0s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g0s RCSB]</span> | |||
}} | }} | ||
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[[Category: Phillips, G N.]] | [[Category: Phillips, G N.]] | ||
[[Category: Schotte, F.]] | [[Category: Schotte, F.]] | ||
[[Category: | [[Category: difference refinement]] | ||
[[Category: | [[Category: intermediate state]] | ||
[[Category: | [[Category: myoglobin]] | ||
[[Category: time-resolved crystallography | [[Category: structure-function relationship]] | ||
[[Category: time-resolved crystallography]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:10:20 2008'' | ||
Revision as of 03:10, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | MB (Physeter catodon) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Unphotolyzed CO-bound L29F Myoglobin, crystal 2
OverviewOverview
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.
About this StructureAbout this Structure
2G0S is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
ReferenceReference
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
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