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   Ribosomal protein L5 has a highly twisted concave surface and flexible
   arms responsible for rRNA binding.
   (PMID:11350033)
     * [23]Abstract This article is available in UKPMC
     * [24]Citations List of citations in UKPMC which this record is cited
       by and<br/> those which it cites
     * [25]BioEntities Biological entities annotated by the EMBL EBI and
       NCBI teams
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       article derived by NCBI <br/>by comparing subject headings and
       words in the title and abstract

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   [28]Nakashima T,
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   [30]Yao M,
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   [32]Kawamura S,
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   [34]Iwasaki K,
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   [36]Kimura M,
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   [38]Tanaka I
   Division of Biological Sciences, Graduate School of Science, Hokkaido
   University, Sapporo, Japan.
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   [40]RNA (New York, N.Y.) [2001, 7(5):692-701]

   Type:  Journal Article, Research Support, Non-U.S. Gov't

   DOI: 10.1017/S1355838201002345 The Digital Object Identifier (DOI)
   System enables identification of digital entities
   Abstract Highlight Terms Highlight biological terms.
   [ ] Gene Ontology(3) [ ] Genes/Proteins(1) [ ] Species(2)

   Ribosomal [41]protein L5 is a [42]5S rRNA binding protein in the large
   subunit and plays an essential role in the promotion of a particular
   conformation of 5S rRNA. The crystal structure of the ribosomal
   [43]protein L5 from [44]Bacillus stearothermophilus has been determined
   at 1.8 A resolution. The molecule consists of a five-stranded
   antiparallel beta-sheet and four alpha-helices, which fold in a way
   that is topologically similar to the ribonucleoprotein (RNP) domain.
   The molecular shape and electrostatic representation suggest that the
   concave surface and loop regions are involved in [45]5S rRNA binding.
   To identify amino acid residues responsible for [46]5S rRNA binding, we
   made use of Ala-scanning [47]mutagenesis of evolutionarily conserved
   amino acids occurring in the beta-strands and loop regions. The
   mutations of Asn37 at the beta1-strand and Gln63 at the loop between
   helix 2 and beta3-strand as well as that of Phe77 at the tip of the
   loop structure between the beta2- and beta3-strands caused a
   significant reduction in [48]5S rRNA binding. In addition, the
   mutations of Thr90 on the beta3-strand and Ile141 and Asp144 at the
   loop between beta4- and beta5-strands moderately reduced the [49]5S
   rRNA-binding affinity. Comparison of these results with the more
   recently analyzed structure of the 50S subunit from [50]Haloarcula
   marismortui suggests that there are significant differences in the
   structure at N- and C-terminal regions and probably in the [51]5S rRNA
   binding.
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