Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic

Science

Volumn 286, Issue 5448, 1999, Pages 2349-2352

  Selmer, Maria ^a   Al Karadaghi, Salam ^a   Hirokawa, Go ^b   Kaji, Akira ^b   Liljas, Anders ^a  

^a LUND UNIVERSITY   (Sweden)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

M PROTEIN; TRANSFER RNA;

ARTICLE; BACTERIUM; MOLECULAR MIMICRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; RIBOSOME;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PEPTIDE ELONGATION FACTOR G; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RIBOSOMAL PROTEINS; RIBOSOMES; RNA, BACTERIAL; RNA, FUNGAL; RNA, TRANSFER; RNA, TRANSFER, PHE; SEQUENCE ALIGNMENT; THERMOTOGA MARITIMA;

BACTERIA (MICROORGANISMS); THERMOTOGA MARITIMA;

EID: 0033579365     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.286.5448.2349     Document Type: Article

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56. We thank P. Lipniunas (Astra-Zeneca, Sweden) for EMS of selenomethionyl RRF, and the tutors and participants in the 3rd European Molecular Biology Organization-sponsored MAD workshop, especially C. Leonard (ESRF, France) and T. Schneider, for assistance with data collection and the search for selenium positions. Native data were collected at the MAX synchrotron at experimental station 711. M.S. is the recipient of a graduate student fellowship from the Swedish Foundation for Strategic Research through SBNet The project was supported by grants to A.L. from the Swedish Natural Science Research Council and the European Union (BIO4-CT97-2188). Coordinates of RRF and structure factor amplitudes have been deposited in the Protein Data Bank (accession code 1dd5).