1SP3

Crystal structure of octaheme cytochrome c from Shewanella oneidensis

Summary for 1SP3

Entry DOI	10.2210/pdb1sp3/pdb
Descriptor	cytochrome c, putative, THIOCYANATE ION, HEME C, ... (4 entities in total)
Functional Keywords	octaheme, cytochrome c, oxidoreductase
Biological source	Shewanella oneidensis
Total number of polymer chains	1
Total formula weight	54577.70
Authors	Mowat, C.G.,Rothery, E.,Miles, C.S.,McIver, L.,Doherty, M.K.,Drewette, K.,Taylor, P.,Walkinshaw, M.D.,Chapman, S.K.,Reid, G.A. (deposition date: 2004-03-16, release date: 2004-09-21, Last modification date: 2024-12-25)
Primary citation	Mowat, C.G.,Rothery, E.,Miles, C.S.,McIver, L.,Doherty, M.K.,Drewette, K.,Taylor, P.,Walkinshaw, M.D.,Chapman, S.K.,Reid, G.A. Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nat.Struct.Mol.Biol., 11:1023-1024, 2004 Cited by PubMed Abstract: 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. PubMed: 15361860 DOI: 10.1038/nsmb827 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation