1abs
From Proteopedia
(New page: 200px<br /><applet load="1abs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1abs, resolution 1.5Å" /> '''PHOTOLYSED CARBONMONO...) |
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| - | [[Image:1abs.jpg|left|200px]]<br /><applet load="1abs" size=" | + | [[Image:1abs.jpg|left|200px]]<br /><applet load="1abs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1abs, resolution 1.5Å" /> | caption="1abs, resolution 1.5Å" /> | ||
'''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K'''<br /> | '''PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Myoglobin is a globular haem protein that reversibly binds ligands such as | + | 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== | ==About this Structure== | ||
| - | 1ABS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ABS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Berendzen, J.]] | [[Category: Berendzen, J.]] | ||
| - | [[Category: Jr., G | + | [[Category: Jr., G N.Phillips.]] |
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
| - | [[Category: Sweet, R | + | [[Category: Sweet, R M.]] |
[[Category: CMO]] | [[Category: CMO]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:57 2008'' |
Revision as of 09:42, 21 February 2008
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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 with , and as ligands. 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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