3DE9

Crystal Structure of a Trimeric Cytochrome cb562 Assembly Induced by Nickel Coordination

3DE9 の概要

• エントリーDOI: 10.2210/pdb3de9/pdb
• 関連するPDBエントリー: 2BC5 2QLA 3DE8
• 分子名称: Soluble cytochrome b562, NICKEL (II) ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: ni-stabilized trimeric superstructure, electron transport, heme, iron, metal-binding, periplasm, transport, metal binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm : P0ABE7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12518.72

構造登録者

Salgado, E.N.,Lewis, R.A.,Rheingold, A.L.,Tezcan, F.A. (登録日: 2008-06-08, 公開日: 2009-04-21, 最終更新日: 2024-02-21)

主引用文献

Salgado, E.N.,Lewis, R.A.,Mossin, S.,Rheingold, A.L.,Tezcan, F.A.
Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination.
Inorg.Chem., 48:2726-2728, 2009

PubMed Abstract: We describe the metal-dependent self-assembly of symmetrical protein homooligomers from protein building blocks that feature appropriately engineered metal-chelating motifs on their surfaces. Crystallographic studies indicate that the same four-helix-bundle protein construct, MBPC-1, can self-assemble into C(2) and C(3) symmetrical assemblies dictated by Cu(II) and Ni(II) coordination, respectively. The symmetry inherent in metal coordination can thus be directly applied to biological self-assembly.

PubMed: 19267481
DOI: 10.1021/ic9001237

実験手法

X-RAY DIFFRACTION (2.04 Å)