3QQ5

Crystal structure of the [FeFe]-hydrogenase maturation protein HydF

3QQ5 の概要

• エントリーDOI: 10.2210/pdb3qq5/pdb
• 関連するPDBエントリー: 1FEH 3CIW 3LX4
• 分子名称: Small GTP-binding protein (1 entity in total)
• 機能のキーワード: hydrogenase, h-cluster, hyda maturation, gtp-binding domain, maturation enzyme, oxidoreductase
• 由来する生物種: Thermotoga neapolitana
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47369.70

構造登録者

Cendron, L.,Berto, P.,D'Adamo, S.,Vallese, F.,Govoni, C.,Posewitz, M.C.,Giacometti, G.M.,Costantini, P.,Zanotti, G. (登録日: 2011-02-15, 公開日: 2011-11-16, 最終更新日: 2024-11-06)

主引用文献

Cendron, L.,Berto, P.,D'Adamo, S.,Vallese, F.,Govoni, C.,Posewitz, M.C.,Giacometti, G.M.,Costantini, P.,Zanotti, G.
Crystal Structure of HydF Scaffold Protein Provides Insights into [FeFe]-Hydrogenase Maturation.
J.Biol.Chem., 286:43944-43950, 2011

PubMed Abstract: [FeFe]-hydrogenases catalyze the reversible production of H2 in some bacteria and unicellular eukaryotes. These enzymes require ancillary proteins to assemble the unique active site H-cluster, a complex structure composed of a 2Fe center bridged to a [4Fe-4S] cubane. The first crystal structure of a key factor in the maturation process, HydF, has been determined at 3 Å resolution. The protein monomer present in the asymmetric unit of the crystal comprises three domains: a GTP-binding domain, a dimerization domain, and a metal cluster-binding domain, all characterized by similar folding motifs. Two monomers dimerize, giving rise to a stable dimer, held together mainly by the formation of a continuous β-sheet comprising eight β-strands from two monomers. Moreover, in the structure presented, two dimers aggregate to form a supramolecular organization that represents an inactivated form of the HydF maturase. The crystal structure of the latter furnishes several clues about the events necessary for cluster generation/transfer and provides an excellent model to begin elucidating the structure/function of HydF in [FeFe]-hydrogenase maturation.

PubMed: 22057316
DOI: 10.1074/jbc.M111.281956

実験手法

X-RAY DIFFRACTION (2.99 Å)