2g0s: Difference between revisions
New page: left|200px<br /><applet load="2g0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g0s, resolution 1.90Å" /> '''Unphotolyzed CO-boun... |
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[[Image:2g0s.gif|left|200px]]<br /><applet load="2g0s" size=" | [[Image:2g0s.gif|left|200px]]<br /><applet load="2g0s" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2g0s, resolution 1.90Å" /> | caption="2g0s, resolution 1.90Å" /> | ||
'''Unphotolyzed CO-bound L29F Myoglobin, crystal 2'''<br /> | '''Unphotolyzed CO-bound L29F Myoglobin, crystal 2'''<br /> | ||
==Overview== | ==Overview== | ||
Picosecond time-resolved crystallography was used to follow the | 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 Structure== | ==About this Structure== | ||
2G0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2G0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0S OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Anfinrud, P | [[Category: Anfinrud, P A.]] | ||
[[Category: Aranda, R.]] | [[Category: Aranda, R.]] | ||
[[Category: Levin, E | [[Category: Levin, E J.]] | ||
[[Category: Phillips, G | [[Category: Phillips, G N.]] | ||
[[Category: Schotte, F.]] | [[Category: Schotte, F.]] | ||
[[Category: CMO]] | [[Category: CMO]] | ||
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[[Category: time-resolved crystallography; myoglobin; difference refinement; structure-function relationship; intermediate states]] | [[Category: time-resolved crystallography; myoglobin; difference refinement; structure-function relationship; intermediate states]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:00 2008'' | ||
Revision as of 18:27, 21 February 2008
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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 with , and as ligands. 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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