Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt 12):993-7. doi: 10.1107/S1744309107061106. Epub 2007 Nov 30.


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 A 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 alpha-helices and six beta-strands, with the beta-strands composing a central beta-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the alpha/beta-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized alpha/beta-hydrolase fold and that an additional component would be required for its activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Humans
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Folding*
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structural Homology, Protein
  • Thermus thermophilus / enzymology*
  • Thermus thermophilus / genetics


  • Hydrolases

Associated data

  • PDB/2DST