2g0r

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[[Image:2g0r.gif|left|200px]]
[[Image:2g0r.gif|left|200px]]
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{{Structure
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|PDB= 2g0r |SIZE=350|CAPTION= <scene name='initialview01'>2g0r</scene>, resolution 1.95&Aring;
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The line below this paragraph, containing "STRUCTURE_2g0r", creates the "Structure Box" on the page.
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|SITE=
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|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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon])
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|DOMAIN=
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{{STRUCTURE_2g0r| PDB=2g0r | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0r OCA], [http://www.ebi.ac.uk/pdbsum/2g0r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g0r RCSB]</span>
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'''Unphotolyzed CO-bound L29F Myoglobin'''
'''Unphotolyzed CO-bound L29F Myoglobin'''
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[[Category: Phillips, G N.]]
[[Category: Phillips, G N.]]
[[Category: Schotte, F.]]
[[Category: Schotte, F.]]
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[[Category: difference refinement]]
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[[Category: Difference refinement]]
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[[Category: intermediate state]]
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[[Category: Intermediate state]]
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[[Category: myoglobin]]
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[[Category: Myoglobin]]
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[[Category: structure-function relationship]]
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[[Category: Structure-function relationship]]
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[[Category: time-resolved crystallography]]
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[[Category: Time-resolved crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:33:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:10:15 2008''
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Revision as of 01:33, 4 May 2008

Template:STRUCTURE 2g0r

Unphotolyzed CO-bound L29F Myoglobin


Overview

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

2G0R is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 04:33:51 2008

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