1NBB

N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C'

Summary for 1NBB

• Entry DOI: 10.2210/pdb1nbb/pdb
• Descriptor: CYTOCHROME C', PROTOPORPHYRIN IX CONTAINING FE, N-BUTYL ISOCYANIDE, ... (4 entities in total)
• Functional Keywords: electron transport, cytochrome, heme protein, electron transport (heme protein)
• Biological source: Rhodobacter capsulatus
• Total number of polymer chains: 2
• Total formula weight: 27708.70

Authors

Tahirov, T.H.,Misaki, S.,Meyer, T.E.,Cusanovich, M.A.,Higuchi, Y.,Yasuoka, N. (deposition date: 1996-03-18, release date: 1996-08-17, Last modification date: 2024-11-20)

Primary citation

Tahirov, T.H.,Misaki, S.,Meyer, T.E.,Cusanovich, M.A.,Higuchi, Y.,Yasuoka, N.
Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c' from rhodobacter capsulatus.
Nat.Struct.Biol., 3:459-464, 1996

PubMed Abstract: We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of amino acid residues in the haem vicinity, accompanied by a rearrangement of the hydrogen bonding pattern. The results suggest that rearrangements resulting from ligand binding could drive dimer dissociation in some species and also that the haem propionate may participate in proton transfer.

PubMed: 8612077
DOI: 10.1038/nsb0596-459

Experimental method

X-RAY DIFFRACTION (2.4 Å)