1e86

From Proteopedia

Revision as of 10:58, 5 November 2007

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

1E86 is a Single protein structure of sequence from Achromobacter xylosoxidans with HEC and CMO as ligands. Structure known Active Sites: CO1, CO2 and HEC. 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 Mon Nov 5 13:03:19 2007