1bzr
From Proteopedia
(New page: 200px<br /><applet load="1bzr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bzr, resolution 1.15Å" /> '''ATOMIC RESOLUTION CR...) |
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| - | [[Image:1bzr.jpg|left|200px]]<br /><applet load="1bzr" size=" | + | [[Image:1bzr.jpg|left|200px]]<br /><applet load="1bzr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bzr, resolution 1.15Å" /> | caption="1bzr, resolution 1.15Å" /> | ||
'''ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE'''<br /> | '''ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of myoglobin in the deoxy- and carbon | + | The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide. |
==About this Structure== | ==About this Structure== | ||
| - | 1BZR 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:// | + | 1BZR 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=1BZR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bartunik, H | + | [[Category: Bartunik, H D.]] |
| - | [[Category: Kachalova, G | + | [[Category: Kachalova, G S.]] |
| - | [[Category: Popov, A | + | [[Category: Popov, A N.]] |
[[Category: CMO]] | [[Category: CMO]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: carbonmonoxy myoglobin]] | [[Category: carbonmonoxy myoglobin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:58 2008'' |
Revision as of 10:01, 21 February 2008
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ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
Overview
The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.
About this Structure
1BZR is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.
Reference
A steric mechanism for inhibition of CO binding to heme proteins., Kachalova GS, Popov AN, Bartunik HD, Science. 1999 Apr 16;284(5413):473-6. PMID:10205052
Page seeded by OCA on Thu Feb 21 12:00:58 2008
