Enzyme structure with two catalytic sites for double-sieve selection of substrate

Science

Volumn 280, Issue 5363, 1998, Pages 578-582

  Nureki, Osamu ^a,b   Vassylyev, Dmitry G ^c   Tateno, Masaru ^a,b   Shimada, Atsushi ^a   Nakama, Takashi ^a   Fukai, Shuya ^a   Konno, Mitiko ^d   Hendrickson, Tamara L ^e   Schimmel, Paul ^e   Yokoyama, Shigeyuki ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^c ADVANCED TELECOMMUNICATIONS RESEARCH INSTITUTE INTERNATIONAL   (Japan)

^d OCHANOMIZU UNIVERSITY   (Japan)

^e SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ISOLEUCINE; ISOLEUCINE TRANSFER RNA LIGASE; VALINE;

AMINOACYLATION; ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; THERMOPHILIC BACTERIUM;

ADENOSINE MONOPHOSPHATE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROGEN BONDING; HYDROLYSIS; ISOLEUCINE; ISOLEUCINE-TRNA LIGASE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RNA, TRANSFER, ILE; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS; TRANSFER RNA AMINOACYLATION; VALINE;

EID: 0032562571     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5363.578     Document Type: Article

References (39)

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39. We thank M. Nakasako, N. Kamiya, M. Yamamoto, H. Iwasaki, T. Ueki, and Y. Maeda for data collection and helpful discussions; N. Watanabe and N. Sakabe for help with synchrotron data collection at the Tsukuba Photon Factory; and K. Nagai and A. Murzin for helpful comments. Supported in part by Grants-in-Aid for Scientific Research on Priority Areas (04272103 and 09278102) to S.Y. from the Ministry of Education, Science, Culture, and Sports of Japan and by grant GM15539 to P.S. and T.H. from NIH. T.H. is an NIH Postdoctoral Fellow. The coordinates for T. thermophilus lleRS have been deposited in the Brookhaven Protein Data Base (1ILE).