1e86: Difference between revisions

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[[Image:1e86.jpg|left|200px]]
{{Seed}}
[[Image:1e86.png|left|200px]]


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{{STRUCTURE_1e86|  PDB=1e86  |  SCENE=  }}  
{{STRUCTURE_1e86|  PDB=1e86  |  SCENE=  }}  


'''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH CO BOUND TO DISTAL SIDE OF HEME'''
===CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH CO BOUND TO DISTAL SIDE OF HEME===




==Overview==
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Microbial cytochromes c' contain a 5-coordinate His-ligated heme that forms stable adducts with nitric oxide (NO) and carbon monoxide (CO), but not with dioxygen. We report the 1.95 and 1.35 A resolution crystal structures of the CO- and NO-bound forms of the reduced protein from Alcaligenes xylosoxidans. NO disrupts the His-Fe bond and binds in a novel mode to the proximal face of the heme, giving a 5-coordinate species. In contrast, CO binds 6-coordinate on the distal side. A second CO molecule, not bound to the heme, is located in the proximal pocket. Since the unusual spectroscopic properties of cytochromes c' are shared by soluble guanylate cyclase (sGC), our findings have potential implications for the activation of sGC induced by the binding of NO or CO to the heme domain.
The line below this paragraph, {{ABSTRACT_PUBMED_11060017}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11060017}}


==About this Structure==
==About this Structure==
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[[Category: Cytochrome]]
[[Category: Cytochrome]]
[[Category: Heme]]
[[Category: Heme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:47:00 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:18:20 2008''

Revision as of 21:18, 30 June 2008

File:1e86.png

Template:STRUCTURE 1e86

CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH CO BOUND TO DISTAL SIDE OF HEME

Template:ABSTRACT PUBMED 11060017

About this Structure

1E86 is a Single protein structure of sequence from Achromobacter xylosoxidans. Full crystallographic information is available from OCA.

Reference

Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase., Lawson DM, Stevenson CE, Andrew CR, Eady RR, EMBO J. 2000 Nov 1;19(21):5661-71. PMID:11060017

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