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

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 63, Issue 12, 2007, Pages 993-997

  Xie, Yong ^a   Takemoto, Chie ^a   Kishishita, Seiichiro ^a   Uchikubo Kamo, Tomomi ^a   Murayama, Kazutaka ^a,b   Chen, Lirong ^c   Liu, Zhi Jie ^c   Wang, Bi Cheng ^c   Manzoku, Miho ^d   Ebihara, Akio ^d   Kuramitsu, Seiki ^d,e   Shirouzu, Mikako ^a   Yokoyama, Shigeyuki ^a,f  

^a RIKEN YOKOHAMA INSTITUTE   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

^c University of Georgia ^*  (United States)

^d Harima Institute ^*  (Japan)

^e OSAKA UNIVERSITY   (Japan)

^f UNIVERSITY OF TOKYO   (Japan)

Author keywords

hydrolase fold; Singleton; T. thermophilus HB8; TTHA1544

Indexed keywords

HYDROLASE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROLASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 36849001374     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309107061106     Document Type: Article

References (20)

1. Argiriadi, M. A., Morisseau, C., Hammock, B. D. & Christianson, D. W. (1999). Proc. Natl Acad. Sci. USA, 96, 10637-10642.
2. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
3. Henne, A. et al. (2004). Nature Biotechnol. 22, 547-553.
4. Holm, L. & Park, J. (2000). Bioinformatics, 16, 566-567.
5. Jones, S. & Thornton, J. M. (1996). Proc. Natl Acad. Sci. USA, 93, 13-20.
6. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
7. Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.
8. Larsen, N. A, Turner, J. M., Stevens, J., Rosser, S. J., Basran, A., Lerner, R. A., Bruce, N. C. & Wilson, I. A. (2002). Nature Struct. Biol. 9, 17-21.
9. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
10. Lawrence, M. C. & Bourke, P. (2000). J. Appl. Cryst. 33, 990-991.
11. LeMaster, D. M. & Richards, F. M. (1985). Biochemistry, 24, 7263-7268.
12. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
13. Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.
14. Nardini, M., Ridder, I. S., Rozeboom, H. J., Kalk, K. H., Rink, R., Janssen, D. B. & Dijkstra, B. W. (1999). J. Biol. Chem. 274, 14579-14586.
15. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 277, 505-524.
16. Padmanabhan, B., Kuzuhara, T., Adachi, N. & Horikoshi, M. (2004). J. Biol. Chem. 279, 9615-9624.
17. Terwilliger, T. C. (2000). Acta Cryst. D56, 965-972.
18. Terwilliger, T. C. & Berendzen, J. (1999). Acta Cryst. D55, 849-861.
19. Vriend, G. (1990). J. Mol. Graph. 8, 52-56.
20. Yokoyama, S., Hirota, H., Kigawa, T., Yabuki, T., Shirouzu, M., Terada, T., Ito, Y., Matsuo, Y., Kuroda, Y., Nishimura, Y., Kyogoku, Y., Miki, K., Masui, R. & Kuramitsu, S. (2000). Nature Struct. Biol. 7, 943-945.