6ZA1
Structure of [NiFeSe] hydrogenase G491A variant from Desulfovibrio vulgaris Hildenborough pressurized with Oxygen gas - structure G491A-O2-hd
6ZA1 の概要
エントリーDOI | 10.2210/pdb6za1/pdb |
分子名称 | Periplasmic [NiFeSe] hydrogenase, small subunit, HYDROSULFURIC ACID, Periplasmic [NiFeSe] hydrogenase, large subunit, selenocysteine-containing, ... (11 entities in total) |
機能のキーワード | hydrogenase, selenium, gas channels, high-pressure derivatization, oxidoreductase |
由来する生物種 | Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 85635.89 |
構造登録者 | Zacarias, S.,Temporao, A.,Carpentier, P.,van der Linden, P.,Pereira, I.A.C.,Matias, P.M. (登録日: 2020-06-04, 公開日: 2020-09-09, 最終更新日: 2024-01-24) |
主引用文献 | Zacarias, S.,Temporao, A.,Carpentier, P.,van der Linden, P.,Pereira, I.A.C.,Matias, P.M. Exploring the gas access routes in a [NiFeSe] hydrogenase using crystals pressurized with krypton and oxygen. J.Biol.Inorg.Chem., 25:863-874, 2020 Cited by PubMed Abstract: Hydrogenases are metalloenzymes that catalyse both H evolution and uptake. They are gas-processing enzymes with deeply buried active sites, so the gases diffuse through channels that connect the active site to the protein surface. The [NiFeSe] hydrogenases are a special class of hydrogenases containing a selenocysteine as a nickel ligand; they are more catalytically active and less O-sensitive than standard [NiFe] hydrogenases. Characterisation of the channel system of hydrogenases is important to understand how the inhibitor oxygen reaches the active site to cause oxidative damage. To this end, crystals of Desulfovibrio vulgaris Hildenborough [NiFeSe] hydrogenase were pressurized with krypton and oxygen, and a method for tracking labile O molecules was developed, for mapping a hydrophobic channel system similar to that of the [NiFe] enzymes as the major route for gas diffusion. PubMed: 32865640DOI: 10.1007/s00775-020-01814-y 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.37 Å) |
構造検証レポート
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