1BCF

THE STRUCTURE OF A UNIQUE, TWO-FOLD SYMMETRIC, HAEM-BINDING SITE

1BCF の概要

• エントリーDOI: 10.2210/pdb1bcf/pdb
• 分子名称: BACTERIOFERRITIN, MANGANESE (II) ION, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: iron storage and electron transport
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 227233.63

構造登録者

Frolow, F.,Kalb(Gilboa), A.J.,Yariv, J. (登録日: 1993-12-06, 公開日: 1994-12-20, 最終更新日: 2024-02-07)

主引用文献

Frolow, F.,Kalb, A.J.,Yariv, J.
Structure of a unique twofold symmetric haem-binding site.
Nat.Struct.Biol., 1:453-460, 1994

PubMed Abstract: Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a hollow, nearly spherical shell made up of 24 identical protein subunits and 12 haems. We have solved this structure in a tetragonal crystal form at 2.9 A resolution. We find that each haem is bound in a pocket formed by the interface between a pair of symmetry-related subunits. The quasi-twofold axis of the haem is closely aligned with the local twofold axis relating these subunits. The axial ligands of the haem are sulphurs of two equivalent methionyl residues (Met 52) from the symmetry-related subunits. A cluster of four water molecules is trapped in the gap between the upper edge of the haem and two extended protein loops which close off the haem from the outer aqueous environment. This is the first structure of a bis-methionine ligated haem-binding site and the first case of a twofold symmetric haem-binding site.

PubMed: 7664064
DOI: 10.1038/nsb0794-453

実験手法

X-RAY DIFFRACTION (2.9 Å)