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

Authors :
Xie Y
Takemoto C
Kishishita S
Uchikubo-Kamo T
Murayama K
Chen L
Liu ZJ
Wang BC
Manzoku M
Ebihara A
Kuramitsu S
Shirouzu M
Yokoyama S
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.

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