1e83: Difference between revisions
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[[Image:1e83. | [[Image:1e83.jpg|left|200px]]<br /><applet load="1e83" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1e83" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1e83, resolution 2.05Å" /> | caption="1e83, resolution 2.05Å" /> | ||
'''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-OXIDIZED STRUCTURE'''<br /> | '''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-OXIDIZED STRUCTURE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1E83 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]. | 1E83 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]. Known structural/functional Site: <scene name='pdbsite=HEC:Hec Binding Site For Chain A'>HEC</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E83 OCA]. | ||
==Reference== | ==Reference== | ||
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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 Dec 18 15:03:23 2007'' | ||
Revision as of 15:53, 18 December 2007
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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 with HEC as ligand. Known structural/functional Site: . 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
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