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嗜热栖热菌HB8最小化α/β-水解酶折叠蛋白的结构

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

作者信息

Xie Yong, Takemoto Chie, Kishishita Seiichiro, Uchikubo-Kamo Tomomi, Murayama Kazutaka, Chen Lirong, Liu Zhi Jie, Wang Bi Cheng, Manzoku Miho, Ebihara Akio, Kuramitsu Seiki, Shirouzu Mikako, Yokoyama Shigeyuki

机构信息

Protein Research Group, Genomic Sciences Center, RIKEN Yokohama Institute, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.

出版信息

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

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.

摘要

编码TTHA1544的基因是嗜热栖热菌HB8基因组中的一个单拷贝基因,编码一种含131个氨基酸的蛋白质。为阐明其功能,采用单波长反常散射法在2.0埃分辨率下测定了TTHA1544的晶体结构。不对称单元中有两个分子。每个分子由四个α螺旋和六条β链组成,β链构成一个中央β折叠片。结构同源性搜索表明,尽管TTHA1544缺乏水解酶的催化残基,但其整体结构类似于α/β水解酶折叠。这些结果表明,TTHA1544代表了最小化的α/β水解酶折叠,其活性还需要一个额外的组分。

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