Decameric SelA•tRNASec ring structure reveals mechanism of bacterial selenocysteine formation

Science

Volumn 340, Issue 6128, 2013, Pages 75-78

  Itoh, Yuzuru ^a,b   Bröcker, Markus J ^c   Sekine, Shun Ichi ^a,b   Hammond, Gifty ^c   Suetsugu, Shiro ^b   Söll, Dieter ^c   Yokoyama, Shigeyuki ^a,b  

^a RIKEN   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL ENZYME; PHOSPHOSERINE; PROTEIN SELA; SELENOCYSTEINE; SYNTHETASE; THIOSULFATE; TRANSFER RNA; UNCLASSIFIED DRUG; AMINOACYL TRANSFER RNA; BACTERIAL PROTEIN; PYRIDOXAL 5 PHOSPHATE; SELENIUM TRANSFERASE; SELENOCYSTEINYL TRNA; SELENOCYSTEINYL-TRNA; TRANSFERASE;

AMINO ACID; CRYSTAL STRUCTURE; ENZYME ACTIVITY; MICROBIAL COMMUNITY; PROTEIN; RNA; SUBSTRATE;

ACYLATION; AMINO ACID SYNTHESIS; AMINO TERMINAL SEQUENCE; AQUIFEX AEOLICUS; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN RNA BINDING; PROTEIN STRUCTURE; RNA BINDING; STRUCTURE ANALYSIS; THERMOANAEROBACTER; THERMOANAEROBACTER TENGCONGENSIS; BACTERIUM; BIOSYNTHESIS; CATALYSIS; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ARGININE; BACTERIA; BACTERIAL PROTEINS; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRIDOXAL PHOSPHATE; RNA, TRANSFER, AMINO ACYL; SELENOCYSTEINE; TRANSFERASES;

MLCS; MLOWN;

EID: 84876314972     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1229521     Document Type: Article

References (14)

1. M. P. Rayman, Lancet 356, 233 (2000).
2. J. E. Cone, R. M. Del Río, J. N. Davis, T. C. Stadtman, Proc. Natl. Acad. Sci. U.S.A. 73, 2659 (1976).
3. A. Böck, M. Thanbichler, M. Rother, A. Resch, in Aminoacyl-tRNA Synthetases, M. Ibba, C. S. Francklyn, S. Cusack, Eds. (Landes Bioscience, Georgetown, TX, 2005), pp. 320-327.
4. B. A. Carlson et al., Proc. Natl. Acad. Sci. U.S.A. 101, 12848 (2004).
5. J. Yuan et al., Proc. Natl. Acad. Sci. U.S.A. 103, 18923 (2006).
6. X. M. Xu et al., PLoS Biol. 5, e4 (2007).
7. A. C. Eliot, J. F. Kirsch, Annu. Rev. Biochem. 73, 383 (2004).
8. S. Palioura, R. L. Sherrer, T. A. Steitz, D. Söll, M. Simonovic, Science 325, 321 (2009).
9. A. Schön, A. Böck, G. Ott, M. Sprinzl, D. Söll, Nucleic Acids Res. 17, 7159 (1989).
10. Y. Itoh, S. Chiba, S. Sekine, S. Yokoyama, Nucleic Acids Res. 37, 6259 (2009).
11. S. Chiba, Y. Itoh, S. Sekine, S. Yokoyama, Mol. Cell 39, 410 (2010).
12. H. Engelhardt, K. Forchhammer, S. Müller, K. N. Goldie, A. Böck, Mol. Microbiol. 6, 3461 (1992).
13. N. Fischer et al., Biol. Chem. 388, 1061 (2007).
14. V. Biou, A. Yaremchuk, M. Tukalo, S. Cusack, Science 263, 1404 (1994).