5JSH
The 3D structure of recombinant [NiFeSe] hydrogenase from Desulfovibrio Vulgaris Hildenborough in the oxidized state at 1.30 Angstrom
5JSH の概要
エントリーDOI | 10.2210/pdb5jsh/pdb |
分子名称 | Periplasmic [NiFeSe] hydrogenase, small subunit, Periplasmic [NiFeSe] hydrogenase, large subunit, selenocysteine-containing, IRON/SULFUR CLUSTER, ... (10 entities in total) |
機能のキーワード | hydrogenase, biological hydrogen production, oxidoreductase |
由来する生物種 | Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 91688.45 |
構造登録者 | |
主引用文献 | Marques, M.C.,Tapia, C.,Gutierrez-Sanz, O.,Ramos, A.R.,Keller, K.L.,Wall, J.D.,De Lacey, A.L.,Matias, P.M.,Pereira, I.A.C. The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis. Nat. Chem. Biol., 13:544-550, 2017 Cited by PubMed Abstract: Hydrogenases are highly active enzymes for hydrogen production and oxidation. [NiFeSe] hydrogenases, in which selenocysteine is a ligand to the active site Ni, have high catalytic activity and a bias for H production. In contrast to [NiFe] hydrogenases, they display reduced H inhibition and are rapidly reactivated after contact with oxygen. Here we report an expression system for production of recombinant [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough and study of a selenocysteine-to-cysteine variant (Sec489Cys) in which, for the first time, a [NiFeSe] hydrogenase was converted to a [NiFe] type. This modification led to severely reduced Ni incorporation, revealing the direct involvement of this residue in the maturation process. The Ni-depleted protein could be partly reconstituted to generate an enzyme showing much lower activity and inactive states characteristic of [NiFe] hydrogenases. The Ni-Sec489Cys variant shows that selenium has a crucial role in protection against oxidative damage and the high catalytic activities of the [NiFeSe] hydrogenases. PubMed: 28319099DOI: 10.1038/nchembio.2335 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.3 Å) |
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