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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
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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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