4RTB

X-ray structure of the FeFe-hydrogenase maturase HydG from Carboxydothermus hydrogenoformans

4RTB の概要

• エントリーDOI: 10.2210/pdb4rtb/pdb
• 分子名称: HydG protein, S-ADENOSYLMETHIONINE, IRON/SULFUR CLUSTER, ... (5 entities in total)
• 機能のキーワード: radical sam enzyme, co/cn synthase, fefe-hydrogenase maturase, lyase
• 由来する生物種: Carboxydothermus hydrogenoformans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55647.26

構造登録者

Nicolet, Y.,Pagnier, A.,Zeppieri, L.,Martin, L.,Amara, P.,Fontecilla-Camps, J.C. (登録日: 2014-11-14, 公開日: 2015-01-28, 最終更新日: 2023-09-20)

主引用文献

Nicolet, Y.,Pagnier, A.,Zeppieri, L.,Martin, L.,Amara, P.,Fontecilla-Camps, J.C.
Crystal Structure of HydG from Carboxydothermus hydrogenoformans: A Trifunctional [FeFe]-Hydrogenase Maturase.
Chembiochem, 16:397-402, 2015

PubMed Abstract: The structure of the radical S-adenosyl-L-methionine (SAM) [FeFe]-hydrogenase maturase HydG involved in CN(-) /CO synthesis is characterized by two internal tunnels connecting its tyrosine-binding pocket with the external medium and the C-terminal Fe4 S4 cluster-containing region. A comparison with a tryptophan-bound NosL structure suggests that substrate binding causes the closing of the first tunnel and, along with mutagenesis studies, that tyrosine binds to HydG with its amino group well positioned for H-abstraction by SAM. In this orientation the dehydroglycine (DHG) fragment caused by tyrosine Cα-Cβ bond scission can readily migrate through the second tunnel towards the C-terminal domain where both CN(-) and CO are synthesized. Our HydG structure appears to be in a relaxed state with its C-terminal cluster CysX2 CysX22 Cys motif exposed to solvent. A rotation of this domain coupled to Fe4 S4 cluster assembly would bury its putatively reactive unique Fe ion thereby allowing it to interact with DHG.

PubMed: 25504963
DOI: 10.1002/cbic.201402661

実験手法

X-RAY DIFFRACTION (2.79 Å)