| Title : Structure of the minimized alpha\/beta-hydrolase fold protein from Thermus thermophilus HB8 - Xie_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_993 |
| 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 |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :993 , 2007 |
| 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. |
| 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 |
| Gene_locus related to this paper: teth8-Q5SI36 |
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 (2007)
Structure of the minimized alpha\/beta-hydrolase fold protein from Thermus thermophilus HB8
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :993
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 (2007)
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :993