1e84
From Proteopedia
(New page: 200px<br /> <applet load="1e84" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e84, resolution 1.90Å" /> '''CYTOCHROME C' FROM ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1E84 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with HEC as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E84 OCA]]. | + | 1E84 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]] with HEC as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: HEC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E84 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11060017 11060017] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11060017 11060017] | ||
| + | [[Category: Achromobacter xylosoxidans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andrew, C.R.]] | [[Category: Andrew, C.R.]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:10:58 2007'' |
Revision as of 09:06, 30 October 2007
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CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE
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
1E84 is a [Single protein] structure of sequence from [Achromobacter xylosoxidans] with HEC as [ligand]. Structure known Active Site: 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
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