Structure Report for: 2DST

Xie, Y., Takemoto, C., Kishishita, S., Uchikubo-Kamo, T., Murayama, K., Chen, L., Liu, Z.J., Wang, B.C., Manzoku, M., Ebihara, A., Kuramitsu, S., Shirouzu, M., Yokoyama, S.

Title: 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 and Yokoyama S <3 more author(s)> 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 (- 3)
Ref: Acta Crystallographica Sect F Struct Biol Cryst Commun, 63:993, 2007 : PubMed
Abstract


ESTHER: Xie_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_993
PubMedSearch: Xie 2007 Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun 63 993
PubMedID: 18084077
Gene_locus related to this paper: teth8-Q5SI36

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.