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| {{STRUCTURE_1abs| PDB=1abs | SCENE= }} | | {{STRUCTURE_1abs| PDB=1abs | SCENE= }} |
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| '''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K'''
| | ===PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_7935843}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7935843 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7935843}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oxygen storage]] | | [[Category: Oxygen storage]] |
| [[Category: Respiratory protein]] | | [[Category: Respiratory protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:04:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:32:54 2008'' |