This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1e85

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:02, 24 December 2014

CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH NO BOUND TO PROXIMAL SIDE OF HEME

Structural highlights

1e85 is a 1 chain structure with sequence from Achromobacter xylosoxidans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1cgo, 1e83, 1e84, 1e86
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CYCP_ALCXX] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lawson DM, Stevenson CE, Andrew CR, Eady RR. Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase. EMBO J. 2000 Nov 1;19(21):5661-71. PMID:11060017 doi:http://dx.doi.org/10.1093/emboj/19.21.5661

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e85"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e85 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e85 RCSB], [http://www.ebi.ac.uk/pdbsum/1e85 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CYCP_ALCXX CYCP_ALCXX]] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1e85

From Proteopedia

Revision as of 22:02, 24 December 2014

CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH NO BOUND TO PROXIMAL SIDE OF HEME

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox