Crystal structure of a conserved ribosomal protein-RNA complex

Science

Volumn 284, Issue 5417, 1999, Pages 1171-1174

  Conn, Graeme L ^a   Draper, David E ^a   Lattman, Eaton E ^b   Gittis, Apostolos G ^b  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN RNA BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE PAIRING; BASE SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PEPTIDE ELONGATION FACTOR G; PEPTIDE ELONGATION FACTORS; PHYLOGENY; PROTEIN CONFORMATION; RIBOSOMAL PROTEINS; RNA, BACTERIAL; RNA, RIBOSOMAL;

EID: 0033553625     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.284.5417.1171     Document Type: Article

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5. 12 with unit cell dimensions a = b = 150.68 Å and c = 63.84 Å. The crystallographic asymmetric unit contains two complexes.
6. A.T. Brünger, Nature 355, 472 (1992)] of 32.1% (1324 reflections) (Table 1). The model contains residues 6 to 72 of L11-C76 and all 58 nucleotides of the RNA. The two complexes in the asymmetric unit have a root-mean-square deviation (rmsd) of 0.60 Å on all protein and RNA backbone atoms (when aligned on Ca and phosphorus). The coordinates have been deposited in the RCSB Protein Databank (accession number 1QA6). Figures 1D, 2A, 2B, and 3B were generated with Setor [S. V. Evans, J. Mol. Graphics 11, 134 (1993)] and Fig. 3C with Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)] and Raster3D [E. A. Merritt and D. J. Bacon, Methods Enzymol. 277, 505 (1997)].
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40. 2-terminus.
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42. Supported by NIH R37 GM29048 (D.E.D.) and the Wellcome Trust, UK (G.L.C.). We are grateful to C. Ogata, D. Cook, C. Foster, D. Karp, and C. Garvie for assistance with data collection and processing. We also thank D. Leahy and M. Bianchet for helpful discussions.