7O1S

Complex-B bound [FeFe]-hydrogenase maturase HydE fromT. Maritima (Wild-type protein)

7O1S の概要

• エントリーDOI: 10.2210/pdb7o1s/pdb
• 関連するPDBエントリー: 7O1O 7O1P
• 分子名称: [FeFe] hydrogenase maturase subunit HydE, S-ADENOSYL-L-HOMOCYSTEINE, IODIDE ION, ... (12 entities in total)
• 機能のキーワード: radical sam protein; hydrogenase maturase; metalloprotein, metal binding protein
• 由来する生物種: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44297.64

構造登録者

Rohac, R.,Martin, L.,Liu, L.,Basu, D.,Tao, L.,Britt, R.D.,Rauchfuss, T.,Nicolet, Y. (登録日: 2021-03-30, 公開日: 2021-05-26, 最終更新日: 2024-01-31)

主引用文献

Rohac, R.,Martin, L.,Liu, L.,Basu, D.,Tao, L.,Britt, R.D.,Rauchfuss, T.B.,Nicolet, Y.
Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B.
J.Am.Chem.Soc., 143:8499-8508, 2021

PubMed Abstract: [FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H into protons and low-potential electrons. It can be best described as a [FeS] cluster coupled to a unique [2Fe] center where the reaction actually takes place. The latter corresponds to two iron atoms, each of which is bound by one CN ligand and one CO ligand. The two iron atoms are connected by a unique azadithiolate molecule (S-CH-NH-CH-S) and an additional bridging CO. This [2Fe] center is built stepwise thanks to the well-orchestrated action of maturating enzymes that belong to the Hyd machinery. Among them, HydG converts l-tyrosine into CO and CN to produce a unique l-cysteine-Fe(CO)CN species termed complex-B. Very recently, HydE was shown to perform radical-based chemistry using synthetic complex-B as a substrate. Here we report the high-resolution crystal structure that establishes the identity of the complex-B-bound HydE. By triggering the reaction prior to crystallization, we trapped a new five-coordinate Fe species, supporting the proposal that HydE performs complex modifications of complex-B to produce a monomeric "SFe(CO)CN" precursor to the [2Fe] center. Substrate access, product release, and intermediate transfer are also discussed.

PubMed: 34048236
DOI: 10.1021/jacs.1c03367

実験手法

X-RAY DIFFRACTION (1.39 Å)