5L31

Crystal structure of an engineered metal-free RIDC1 variant containing five disulfide bonds.

5L31 の概要

• エントリーDOI: 10.2210/pdb5l31/pdb
• 分子名称: Soluble cytochrome b562, HEME C, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: engineered protein, cytochrome, complex, electron transport
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49364.86

構造登録者

Tezcan, F.A.,Churchfield, L.A. (登録日: 2016-08-02, 公開日: 2016-11-09, 最終更新日: 2024-11-06)

主引用文献

Churchfield, L.A.,Medina-Morales, A.,Brodin, J.D.,Perez, A.,Tezcan, F.A.
De Novo Design of an Allosteric Metalloprotein Assembly with Strained Disulfide Bonds.
J.Am.Chem.Soc., 138:13163-13166, 2016

PubMed Abstract: A major goal in metalloprotein design is to build protein scaffolds from scratch that allow precise control over metal coordination. A particular challenge in this regard is the construction of allosteric systems in which metal coordination equilibria are coupled to other chemical events that take place elsewhere in the protein scaffold. We previously developed a metal-templated self-assembly strategy (MeTIR) to build supramolecular protein complexes with tailorable interfaces from monomeric building blocks. Here, using this strategy, we have incorporated multiple disulfide bonds into the interfaces of a Zn-templated cytochrome cb assembly in order to create mechanical strain on the quaternary structural level. Structural and biophysical analyses indicate that this strain leads to an allosteric system in which Zn binding and dissociation are remotely coupled to the formation and breakage of a disulfide bond over a distance of >14 Å. The breakage of this strained bond upon Zn dissociation occurs in the absence of any reductants, apparently through a hydrolytic mechanism that generates a sulfenic acid/thiol pair.

PubMed: 27649076
DOI: 10.1021/jacs.6b08458

実験手法

X-RAY DIFFRACTION (2.4 Å)