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


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.

SUBMITTER: Xie Y 

PROVIDER: S-EPMC2344104 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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

Xie Yong Y   Takemoto Chie C   Kishishita Seiichiro S   Uchikubo-Kamo Tomomi T   Murayama Kazutaka K   Chen Lirong L   Liu Zhi Jie ZJ   Wang Bi Cheng BC   Manzoku Miho M   Ebihara Akio A   Kuramitsu Seiki S   Shirouzu Mikako M   Yokoyama Shigeyuki S  

Acta crystallographica. Section F, Structural biology and crystallization communications 20071130 Pt 12


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  ...[more]

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