5JSY

The 3D structure of the Ni-reconstituted U489C variant of [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough at 1.04 Angstrom resolution

5JSY の概要

• エントリーDOI: 10.2210/pdb5jsy/pdb
• 分子名称: Periplasmic [NiFeSe] hydrogenase, small subunit, Periplasmic [NiFeSe] hydrogenase, large subunit, selenocysteine-containing, IRON/SULFUR CLUSTER, ... (9 entities in total)
• 機能のキーワード: nifese-site h2 cleavage/production, oxidoreductase
• 由来する生物種: Desulfovibrio vulgaris str. Hildenborough; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91273.91

構造登録者

Marques, M.C.,Pereira, I.A.C.,Matias, P.M. (登録日: 2016-05-09, 公開日: 2017-03-22, 最終更新日: 2024-01-10)

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

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: 28319099
DOI: 10.1038/nchembio.2335

実験手法

X-RAY DIFFRACTION (1.04 Å)