1e85
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Microbial cytochromes c' contain a 5-coordinate His-ligated heme that | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Achromobacter xylosoxidans]] | [[Category: Achromobacter xylosoxidans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Andrew, C | + | [[Category: Andrew, C R.]] |
| - | [[Category: Eady, R | + | [[Category: Eady, R R.]] |
| - | [[Category: Lawson, D | + | [[Category: Lawson, D M.]] |
| - | [[Category: Stevenson, C | + | [[Category: Stevenson, C E.M.]] |
[[Category: HEC]] | [[Category: HEC]] | ||
[[Category: NO]] | [[Category: NO]] | ||
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[[Category: nitric oxide]] | [[Category: nitric oxide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:54 2008'' |
Revision as of 10:24, 21 February 2008
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CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH NO BOUND TO PROXIMAL SIDE OF HEME
Overview
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 Structure
1E85 is a Single protein structure of sequence from Achromobacter xylosoxidans with and as ligands. Known structural/functional Sites: and . 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
Page seeded by OCA on Thu Feb 21 12:24:54 2008
