Structure of the putative thioesterase protein TTHA1846 from Thermus thermophilus HB8 complexed with coenzyme A and a zinc ion

Toshiaki Hosaka, Kazutaka Murayama, Miyuki Kato-Murayama, Akiko Urushibata, Ryogo Akasaka, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

TTHA1846 is a conserved hypothetical protein from Thermus thermophilus HB8 with a molecular mass of 15.1 kDa that belongs to the thioesterase superfamily (Pfam 03061). Here, the 1.9 Å resolution crystal structure of TTHA1846 from T. thermophilus is reported. The crystal structure is a dimer of dimers. Each subunit adopts the so-called hot-dog fold composed of five antiparallel Β-strands flanked on one side by a rather long -helix and shares structural similarity to a number of thioesterases. Unexpectedly, TTHA1846 binds one metal ion and one ligand per subunit. The ligand density was modelled as coenzyme A (CoA). Its structure was confirmed by MALDI-TOF mass spectrometry and electron-density mapping. X-ray absorption fine-structure (XAFS) measurement of the crystal unambiguously characterized the metal ion as zinc. The zinc ion is tetrahedrally coordinated by the side chains of Asp18, His22 and Glu50 and the CoA thiol group. This is the first structural report of the interaction of CoA with a zinc ion. From structural and database analyses, it was speculated that the zinc ion may play an inhibitory role in the enzymatic activity.

Original languageEnglish
Pages (from-to)767-776
Number of pages10
JournalActa Crystallographica Section D: Biological Crystallography
Volume65
Issue number8
DOIs
Publication statusPublished - 2009 Aug 14

Keywords

  • Coenzyme A
  • Hot-dog fold
  • Thermus thermophilus
  • Thioesterases
  • Zinc ion

ASJC Scopus subject areas

  • Structural Biology

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