3HNL

Crystal structure of the Cu-induced dimer of the engineered cyt cb562 variant RIDC-1

3HNL の概要

• エントリーDOI: 10.2210/pdb3hnl/pdb
• 関連するPDBエントリー: 2BC5 2QLA 3HNI 3HNJ 3HNK
• 分子名称: Soluble cytochrome b562, PROTOPORPHYRIN IX CONTAINING FE, COPPER (II) ION, ... (5 entities in total)
• 機能のキーワード: electron 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: 2
• 化学式量合計: 24829.14

構造登録者

Salgado, E.N.,Lewis, R.A.,Brodin, J.,Tezcan, F.A. (登録日: 2009-05-31, 公開日: 2010-02-09, 最終更新日: 2023-09-06)

主引用文献

Salgado, E.N.,Ambroggio, X.I.,Brodin, J.D.,Lewis, R.A.,Kuhlman, B.,Tezcan, F.A.
Metal templated design of protein interfaces.
Proc.Natl.Acad.Sci.USA, 107:1827-1832, 2010

PubMed Abstract: Metal coordination is a key structural and functional component of a large fraction of proteins. Given this dual role we considered the possibility that metal coordination may have played a templating role in the early evolution of protein folds and complexes. We describe here a rational design approach, Metal Templated Interface Redesign (MeTIR), that mimics the time course of a hypothetical evolutionary pathway for the formation of stable protein assemblies through an initial metal coordination event. Using a folded monomeric protein, cytochrome cb(562), as a building block we show that its non-self-associating surface can be made self-associating through a minimal number of mutations that enable Zn coordination. The protein interfaces in the resulting Zn-directed, D(2)-symmetrical tetramer are subsequently redesigned, yielding unique protein architectures that self-assemble in the presence or absence of metals. Aside from its evolutionary implications, MeTIR provides a route to engineer de novo protein interfaces and metal coordination environments that can be tuned through the extensive noncovalent bonding interactions in these interfaces.

PubMed: 20080561
DOI: 10.1073/pnas.0906852107

実験手法

X-RAY DIFFRACTION (2.2 Å)