Literature DB >> 18084077

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

Yong Xie1, 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.   

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.

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Year:  2007        PMID: 18084077      PMCID: PMC2344104          DOI: 10.1107/S1744309107061106

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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