5L32
Crystal structure of the Zn-RIDC1 complex bearing six interfacial disulfide bonds
5L32 の概要
| エントリーDOI | 10.2210/pdb5l32/pdb |
| 関連するPDBエントリー | 5L31 |
| 分子名称 | Soluble cytochrome b562, HEME C, HEXAETHYLENE GLYCOL, ... (5 entities in total) |
| 機能のキーワード | protein engineering, metalloprotein, cytochrome, disulfide bonding, 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 | 4 |
| 化学式量合計 | 49846.85 |
| 構造登録者 | |
| 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 Cited by 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: 27649076DOI: 10.1021/jacs.6b08458 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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