3VX3

Crystal structure of [NiFe] hydrogenase maturation protein HypB from Thermococcus kodakarensis KOD1

3VX3 の概要

• エントリーDOI: 10.2210/pdb3vx3/pdb
• 分子名称: ATPase involved in chromosome partitioning, ParA/MinD family, Mrp homolog, ADENOSINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: mrp/mind family atpase, [nife] hydrogenase maturation, adp binding protein
• 由来する生物種: Thermococcus kodakarensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56470.90

構造登録者

Sasaki, D.,Watanabe, S.,Miki, K. (登録日: 2012-09-09, 公開日: 2013-02-27, 最終更新日: 2024-03-20)

主引用文献

Sasaki, D.,Watanabe, S.,Matsumi, R.,Shoji, T.,Yasukochi, A.,Tagashira, K.,Fukuda, W.,Kanai, T.,Atomi, H.,Imanaka, T.,Miki, K.
Identification and Structure of a Novel Archaeal HypB for [NiFe] Hydrogenase Maturation
J.Mol.Biol., 425:1627-1640, 2013

PubMed Abstract: HypB (metal-binding GTPase) and HypA (nickel metallochaperone) are required for nickel insertion into [NiFe] hydrogenase. However, the HypB homolog proteins are not found in some archaeal species including Thermococcales. In this article, we identify a novel archaeal Mrp/MinD family ATPase-type HypB from Thermococcus kodakarensis (Tk-mmHypB) and determine its crystal structure. The mmhypB gene is conserved among species lacking the hypB gene and is located adjacent to the hypA gene on their genome. Deletion of the mmhypB gene leads to a significant reduction in hydrogen-dependent growth of T. kodakarensis, which is restored by nickel supplementation. The monomer structure of Tk-mmHypB is similar to those of the Mrp/MinD family ATPases. The ADP molecules are tightly bound to the protein. Isothermal titration calorimetry shows that Tk-mmHypB binds ATP with a K(d) value of 84 nM. ADP binds more tightly than does ATP, with a K(d) value of 15 nM. The closed Tk-mmHypB dimer in the crystallographic asymmetric unit is consistent with the ATP-hydrolysis-deficient dimer of the Mrp/MinD family Soj/MinD proteins. Structural comparisons with these proteins suggest the ATP-binding dependent conformational change and rearrangement of the Tk-mmHypB dimer. These observations imply that the nickel insertion process during the [NiFe] hydrogenase maturation is performed by HypA, mmHypB, and a nucleotide exchange factor in these archaea.

PubMed: 23399544
DOI: 10.1016/j.jmb.2013.02.004

実験手法

X-RAY DIFFRACTION (2.1 Å)