1e84
From Proteopedia
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| - | [[Image:1e84.jpg|left|200px]] | + | [[Image:1e84.jpg|left|200px]] |
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| - | '''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE''' | + | {{Structure |
| + | |PDB= 1e84 |SIZE=350|CAPTION= <scene name='initialview01'>1e84</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=HEC:Hec+Binding+Site+For+Chain+A'>HEC</scene> | ||
| + | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E84 is a [ | + | 1E84 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/11060017 11060017] |
[[Category: Achromobacter xylosoxidans]] | [[Category: Achromobacter xylosoxidans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:26 2008'' |
Revision as of 08:51, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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