Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1

Sunghark Kwon, Yuichi Nishitani, Satoshi Watanabe, Yoshinori Hirao, Tadayuki Imanaka, Tamotsu Kanai, Haruyuki Atomi, Kunio Miki

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

A [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1 (TkHybD) is involved in the cleavage of the C-terminal residues of [NiFe] hydrogenase large subunits by Ni recognition. Here, we report the crystal structure of TkHybD at 1.82 Å resolution to better understand this process. TkHybD exhibits an α/β/α sandwich fold with conserved residues responsible for the Ni recognition. Comparisons of TkHybD with homologous proteins also reveal that they share a common overall architecture, suggesting that they have similar catalytic functions. Our results including metal binding site prediction provide insight into the substrate recognition and catalysis mechanism of TkHybD. Proteins 2016; 84:1321–1327.

Original languageEnglish
Pages (from-to)1321-1327
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Volume84
Issue number9
DOIs
Publication statusPublished - 2016 Sep 1

Keywords

  • C-terminal cleavage
  • Ni binding
  • hyperthermophilic archaea
  • protease
  • substrate recognition

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Crystal structure of a [NiFe] hydrogenase maturation protease HybD from Thermococcus kodakarensis KOD1'. Together they form a unique fingerprint.

  • Cite this