1e83: Difference between revisions
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'''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-OXIDIZED STRUCTURE''' | '''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-OXIDIZED STRUCTURE''' | ||
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[[Category: Stevenson, C E.M.]] | [[Category: Stevenson, C E.M.]] | ||
[[Category: 4-helix bundle]] | [[Category: 4-helix bundle]] | ||
[[Category: | [[Category: Cytochrome]] | ||
[[Category: | [[Category: Heme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:46:49 2008'' | |||
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Revision as of 14:46, 2 May 2008
CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-OXIDIZED STRUCTURE
OverviewOverview
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.
About this StructureAbout this Structure
1E83 is a Single protein structure of sequence from Achromobacter xylosoxidans. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 14:46:49 2008