1sp3
Crystal structure of octaheme cytochrome c from Shewanella oneidensis
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | SO4144 (tigr locus) (Bacteria) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.
About this StructureAbout this Structure
1SP3 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
ReferenceReference
Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation., Mowat CG, Rothery E, Miles CS, McIver L, Doherty MK, Drewette K, Taylor P, Walkinshaw MD, Chapman SK, Reid GA, Nat Struct Mol Biol. 2004 Oct;11(10):1023-4. Epub 2004 Sep 7. PMID:15361860
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