Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8

Yong Xie, Chie Takemoto, Seiichiro Kishishita, Tomomi Uchikubo-Kamo, Kazutaka Murayama, Lirong Chen, Zhi Jie Liu, Bi Cheng Wang, Miho Manzoku, Akio Ebihara, Seiki Kuramitsu, Mikako Shirouzu, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

The gene encoding TTHA1544 is a singleton found in the Thermus thermophilus HB8 genome and encodes a 131-amino-acid protein. The crystal structure of TTHA1544 has been determined at 2.0 Å resolution by the single-wavelength anomalous dispersion method in order to elucidate its function. There are two molecules in the asymmetric unit. Each molecule consists of four α-helices and six β-strands, with the β-strands composing a central β-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the α/β-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized α/β-hydrolase fold and that an additional component would be required for its activity.

Original languageEnglish
Pages (from-to)993-997
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number12
DOIs
Publication statusPublished - 2007 Nov 30

Keywords

  • Singleton
  • T. thermophilus HB8
  • TTHA1544
  • α/β-hydrolase fold

ASJC Scopus subject areas

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

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