Structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, at 2.4 Å resolution: A putative member of the StAR-related lipid-transfer (START) domain superfamily

Makoto Nakabayashi, Naoki Shibata, Hirofumi Komori, Yasufumi Ueda, Hitoshi Iino, Akio Ebihara, Seiki Kuramitsu, Yoshiki Higuchi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The crystal structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, has been determined at 2.4 Å resolution as a part of a structural and functional genomics project on T. thermophilus HB8. The main-chain folding shows a compact α+β motif, forming a hydrophobic cavity in the molecule. A structural similarity search reveals that it resembles those steroidogenic acute regulatory proteins that contain the lipid-transfer (START) domain, even though TTHA0849 shows comparatively weak sequence identity to polyketide cyclases. However, the size of the ligand-binding cavity is distinctly smaller than other START domain-containing proteins, suggesting that it catalyses the transfer of smaller ligand molecules.

Original languageEnglish
Pages (from-to)1027-1031
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number12
DOIs
Publication statusPublished - Dec 1 2005

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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