1abs
From Proteopedia
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|PDB= 1abs |SIZE=350|CAPTION= <scene name='initialview01'>1abs</scene>, resolution 1.5Å | |PDB= 1abs |SIZE=350|CAPTION= <scene name='initialview01'>1abs</scene>, resolution 1.5Å | ||
|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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Sweet, R M.]] | [[Category: Sweet, R M.]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SO4]] | ||
[[Category: intermediate in ligand binding]] | [[Category: intermediate in ligand binding]] | ||
[[Category: oxygen storage]] | [[Category: oxygen storage]] | ||
[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:10 2008'' |
Revision as of 15:37, 30 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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