| Literature DB >> 18084077 |
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.Entities:
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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