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1abs

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[[Image:1abs.jpg|left|200px]]
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{{Structure
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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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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1abs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abs OCA], [http://www.ebi.ac.uk/pdbsum/1abs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1abs RCSB]</span>
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'''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K'''
'''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K'''
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[[Category: Schlichting, I.]]
[[Category: Schlichting, I.]]
[[Category: Sweet, R M.]]
[[Category: Sweet, R M.]]
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[[Category: intermediate in ligand binding]]
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[[Category: Intermediate in ligand binding]]
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[[Category: oxygen storage]]
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[[Category: Oxygen storage]]
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[[Category: respiratory protein]]
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[[Category: Respiratory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:04:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:10 2008''
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Revision as of 07:04, 2 May 2008

Image:1abs.jpg

Template:STRUCTURE 1abs

PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K


Overview

Myoglobin is a globular haem protein that reversibly binds ligands such as O2 and CO. Single photons of visible light can break the covalent bond between CO and the haem iron in carbon-monoxy-myoglobin (MbCO) and thus form an unstable intermediate, Mb*CO, with the CO inside the protein. The ensuing rebinding process has been extensively studied as a model for the interplay of dynamics, structure and function in protein reactions. We have used X-ray crystallography at liquid-helium temperatures to determine the structure of Mb*CO to a resolution of 1.5 A. The photodissociated CO lies on top of the haem pyrrole ring C. Comparison with the CO-bound and unligated myoglobin structures reveals that on photodissociation of the CO, the haem 'domes', the iron moves partially out of the haem plane, the iron-proximal histidine bonds is compressed, the F helix is strained and the distal histidine swings towards the outside of the ligand-binding pocket.

About this Structure

1ABS is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

Crystal structure of photolysed carbonmonoxy-myoglobin., Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM, Nature. 1994 Oct 27;371(6500):808-12. PMID:7935843 Page seeded by OCA on Fri May 2 10:04:49 2008

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