Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8

Yong Xie; 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

doi:10.1107/S1744309107061106

Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8

Yong Xie, 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

MEN - Biomedical Engineering

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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 Å 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 α-helices and six β-strands, with the β-strands composing a central β-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the α/β-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized α/β-hydrolase fold and that an additional component would be required for its activity.

Original language	English
Pages (from-to)	993-997
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	12
DOIs	https://doi.org/10.1107/S1744309107061106
Publication status	Published - 2007 Nov 30

Keywords

Singleton
T. thermophilus HB8
TTHA1544
α/β-hydrolase fold

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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. (2007). Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(12), 993-997. https://doi.org/10.1107/S1744309107061106

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title = "Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8",

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 {\AA} 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 α-helices and six β-strands, with the β-strands composing a central β-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the α/β-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized α/β-hydrolase fold and that an additional component would be required for its activity.",

keywords = "Singleton, T. thermophilus HB8, TTHA1544, α/β-hydrolase fold",

author = "Yong Xie and Chie Takemoto and Seiichiro Kishishita and Tomomi Uchikubo-Kamo and Kazutaka Murayama and Lirong Chen and Liu, {Zhi Jie} and Wang, {Bi Cheng} and Miho Manzoku and Akio Ebihara and Seiki Kuramitsu and Mikako Shirouzu and Shigeyuki Yokoyama",

year = "2007",

month = nov,

day = "30",

doi = "10.1107/S1744309107061106",

language = "English",

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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 α/β-hydrolase fold protein from Thermus thermophilus HB8', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 12, pp. 993-997. https://doi.org/10.1107/S1744309107061106

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T1 - Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8

AU - Xie, Yong

AU - Takemoto, Chie

AU - Kishishita, Seiichiro

AU - Uchikubo-Kamo, Tomomi

AU - Murayama, Kazutaka

AU - Chen, Lirong

AU - Liu, Zhi Jie

AU - Wang, Bi Cheng

AU - Manzoku, Miho

AU - Ebihara, Akio

AU - Kuramitsu, Seiki

AU - Shirouzu, Mikako

AU - Yokoyama, Shigeyuki

PY - 2007/11/30

Y1 - 2007/11/30

N2 - 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 Å 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 α-helices and six β-strands, with the β-strands composing a central β-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the α/β-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized α/β-hydrolase fold and that an additional component would be required for its activity.

AB - 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 Å 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 α-helices and six β-strands, with the β-strands composing a central β-sheet. A structural homology search revealed that the overall structure of TTHA1544 resembles the α/β-hydrolase fold, although TTHA1544 lacks the catalytic residues of a hydrolase. These results suggest that TTHA1544 represents the minimized α/β-hydrolase fold and that an additional component would be required for its activity.

KW - Singleton

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ER -

Structure of the minimized α/β-hydrolase fold protein from Thermus thermophilus HB8

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Keywords

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