1sp3

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Crystal structure of octaheme cytochrome c from Shewanella oneidensisCrystal structure of octaheme cytochrome c from Shewanella oneidensis

Structural highlights

1sp3 is a 1 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8E9W8_SHEON

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

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.

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[1]

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

References

  1. Mowat CG, Rothery E, Miles CS, McIver L, Doherty MK, Drewette K, Taylor P, Walkinshaw MD, Chapman SK, Reid GA. Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nat Struct Mol Biol. 2004 Oct;11(10):1023-4. Epub 2004 Sep 7. PMID:15361860 doi:10.1038/nsmb827

1sp3, resolution 2.20Å

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OCA