Crystal Structure of HypA, a Nickel-Binding Metallochaperone for [NiFe] Hydrogenase Maturation

Satoshi Watanabe, Takayuki Arai, Rie Matsumi, Haruyuki Atomi, Tadayuki Imanaka, Kunio Miki

研究成果: ジャーナルへの寄稿学術誌査読

57 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)448-459
ページ数12
ジャーナルJournal of Molecular Biology
394
3
DOI
出版ステータス出版済み - 12月 4 2009
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 分子生物学

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