2g14: Difference between revisions

Revision as of 12:37, 10 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2g14.png

Template:STRUCTURE 2g14

Photolyzed CO L29F Myoglobin: 3.16usPhotolyzed CO L29F Myoglobin: 3.16us

Template:ABSTRACT PUBMED 16790933

About this StructureAbout this Structure

2G14 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Photolyzed CO L29F Myoglobin: 3.16us'''
+===Photolyzed CO L29F Myoglobin: 3.16us===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16790933}}, adds the Publication Abstract to the page
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 [[Category: Structure-function relationship]]
 [[Category: Time-resolved crystallography]]
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