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  • Title: Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8.
    Author: 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.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2007 Dec 01; 63(Pt 12):993-7. PubMed ID: 18084077.
    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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