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1bz6

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{{STRUCTURE_1bz6| PDB=1bz6 | SCENE= }}
{{STRUCTURE_1bz6| PDB=1bz6 | SCENE= }}
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'''ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE'''
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===ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10205052 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10205052}}
==About this Structure==
==About this Structure==
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[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
[[Category: Respiratory protein]]
[[Category: Respiratory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:08:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:59:02 2008''

Revision as of 16:59, 30 June 2008

Image:1bz6.png

Template:STRUCTURE 1bz6

ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE

Template:ABSTRACT PUBMED 10205052

About this Structure

1BZ6 is a Single protein structure of sequence from Physeter catodon. 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 Mon Jun 30 19:59:02 2008

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