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Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2007 Dec 01; Vol. 63 (Pt 12), pp. 993-7. Date of Electronic Publication: 2007 Nov 30. - Publication Year :
- 2007
-
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 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.
- Subjects :
- Amino Acid Sequence
Crystallography, X-Ray
Humans
Hydrolases genetics
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Sequence Alignment
Sequence Homology, Amino Acid
Structural Homology, Protein
Thermus thermophilus genetics
Hydrolases chemistry
Hydrolases metabolism
Protein Folding
Thermus thermophilus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 63
- Issue :
- Pt 12
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 18084077
- Full Text :
- https://doi.org/10.1107/S1744309107061106