1NBB

N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C'

1NBB の概要

• エントリーDOI: 10.2210/pdb1nbb/pdb
• 分子名称: CYTOCHROME C', PROTOPORPHYRIN IX CONTAINING FE, N-BUTYL ISOCYANIDE, ... (4 entities in total)
• 機能のキーワード: electron transport, cytochrome, heme protein, electron transport (heme protein)
• 由来する生物種: Rhodobacter capsulatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27708.70

構造登録者

Tahirov, T.H.,Misaki, S.,Meyer, T.E.,Cusanovich, M.A.,Higuchi, Y.,Yasuoka, N. (登録日: 1996-03-18, 公開日: 1996-08-17, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)