This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 14: | Line 14: | ||
[[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]] | ||
| Line 24: | Line 24: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 11:42:57 2008
