2dst | pdb_00002dst
From Proteopedia
Crystal Structure Analysis of TT1977
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Structural highlights
Publication Abstract from PubMedThe 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. Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8.,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 Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt, 12):993-7. Epub 2007 Nov 30. PMID:18084077[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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