3A44

Crystal structure of HypA in the dimeric form

3A44 の概要

• エントリーDOI: 10.2210/pdb3a44/pdb
• 関連するPDBエントリー: 3A43
• 分子名称: Hydrogenase nickel incorporation protein hypA, ZINC ION (2 entities in total)
• 機能のキーワード: [nife] hydrogenase maturation, zinc-finger, nickel binding, domain swapping, metal-binding, nickel, metal binding protein
• 由来する生物種: Pyrococcus kodakaraensis (Thermococcus kodakaraensis)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63221.59

構造登録者

Watanabe, S.,Arai, T.,Matsumi, R.,Atomi, H.,Imanaka, T.,Miki, K. (登録日: 2009-06-30, 公開日: 2009-10-06, 最終更新日: 2024-11-13)

主引用文献

Watanabe, S.,Arai, T.,Matsumi, R.,Atomi, H.,Imanaka, T.,Miki, K.
Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation.
J.Mol.Biol., 394:448-459, 2009

PubMed Abstract: HypA is one of the auxiliary proteins involved in the maturation of [NiFe] hydrogenases. By an unknown mechanism, HypA functions as a metallochaperone in the insertion of the Ni atom into hydrogenases. We have determined the crystal structures of HypA from Thermococcus kodakaraensis KOD1 in both monomeric and dimeric states. The structure of the HypA monomer consists of Ni- and Zn-binding domains. The relative arrangement of the two metal-binding domains has been shown to be associated with local conformations of the conserved Ni-binding motif, suggesting a communication between the Ni- and Zn-binding sites. The HypA dimer has been shown to be stabilized by unexpected domain swapping through archaea-specific linker helices. In addition, the hexameric structure of HypA is formed in the crystal packing. Several hydrogen bonds and hydrophobic interactions stabilize the hexamer interface. These findings suggest the functional diversity of HypA proteins.

PubMed: 19769985
DOI: 10.1016/j.jmb.2009.09.030

実験手法

X-RAY DIFFRACTION (3.31 Å)