1bzr
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(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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Revision as of 09:55, 20 November 2007
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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 SO4, HEM and CMO 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
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