1e86
From Proteopedia
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| - | [[Image:1e86.jpg|left|200px]]<br /><applet load="1e86" size=" | + | [[Image:1e86.jpg|left|200px]]<br /><applet load="1e86" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e86, resolution 1.95Å" /> | caption="1e86, resolution 1.95Å" /> | ||
'''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH CO BOUND TO DISTAL SIDE OF HEME'''<br /> | '''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH CO BOUND TO DISTAL SIDE OF HEME'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E86 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 and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=CO1:Cmo Binding Site For Chain A'>CO1</scene>, <scene name='pdbsite=CO2:Cmo Binding Site For Chain A'>CO2</scene> and <scene name='pdbsite=HEC:Hec Binding Site For Chain A'>HEC</scene>. Full crystallographic information is available from [http:// | + | 1E86 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 <scene name='pdbligand=HEC:'>HEC</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=CO1:Cmo+Binding+Site+For+Chain+A'>CO1</scene>, <scene name='pdbsite=CO2:Cmo+Binding+Site+For+Chain+A'>CO2</scene> and <scene name='pdbsite=HEC:Hec+Binding+Site+For+Chain+A'>HEC</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E86 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:38:11 2008'' |
Revision as of 07:38, 3 February 2008
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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 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
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