2HF8

Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form, in complex with zinc

2HF8 の概要

• エントリーDOI: 10.2210/pdb2hf8/pdb
• 分子名称: Probable hydrogenase nickel incorporation protein hypB, MAGNESIUM ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: alpha and beta protein, p-loop containing nucleoside triphosphate hydrolase, hydrolase, metal binding protein
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51365.60

構造登録者

Gasper, R.,Scrima, A.,Wittinghofer, A. (登録日: 2006-06-23, 公開日: 2006-07-04, 最終更新日: 2024-11-13)

主引用文献

Gasper, R.,Scrima, A.,Wittinghofer, A.
Structural insights into HypB, a GTP-binding protein that regulates metal binding.
J.Biol.Chem., 281:27492-27502, 2006

PubMed Abstract: HypB is a prokaryotic metal-binding guanine nucleotide-binding protein that is essential for nickel incorporation into hydrogenases. Here we solved the x-ray structure of HypB from Methanocaldococcus jannaschii. It shows that the G-domain has a different topology than the Ras-like proteins and belongs to the SIMIBI (after Signal Recognition Particle, MinD and BioD) class of NTP-binding proteins. We show that HypB undergoes nucleotide-dependent dimerization, which is apparently a common feature of SIMIBI class G-proteins. The nucleotides are located in the dimer interface and are contacted by both subunits. The active site features residues from both subunits arguing that hydrolysis also requires dimerization. Two metal-binding sites are found, one of which is dependent on the state of bound nucleotide. A totally conserved ENV/IGNLV/ICP motif in switch II relays the nucleotide binding with the metal ionbinding site. The homology with NifH, the Fe protein subunit of nitrogenase, suggests a mechanistic model for the switch-dependent incorporation of a metal ion into hydrogenases.

PubMed: 16807243
DOI: 10.1074/jbc.M600809200

実験手法

X-RAY DIFFRACTION (2.1 Å)