1abs
From Proteopedia
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| - | [[Image:1abs.jpg|left|200px]] | + | [[Image:1abs.jpg|left|200px]] |
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| - | '''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K''' | + | {{Structure |
| + | |PDB= 1abs |SIZE=350|CAPTION= <scene name='initialview01'>1abs</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ABS is a [ | + | 1ABS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABS OCA]. |
==Reference== | ==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:[http:// | + | Crystal structure of photolysed carbonmonoxy-myoglobin., Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM, Nature. 1994 Oct 27;371(6500):808-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7935843 7935843] |
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:55:30 2008'' |
Revision as of 07:55, 20 March 2008
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| , resolution 1.5Å | |||||||
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| Ligands: | , and | ||||||
| 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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