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The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl‐tRNA synthetases
Author(s) -
Stoldt Matthias,
Wöhnert Jens,
Görlach Matthias,
Brown Larry R.
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.21.6377
Subject(s) - biology , ribosomal protein , escherichia coli , homology (biology) , transfer rna , ribosomal rna , biochemistry , microbiology and biotechnology , genetics , ribosome , amino acid , rna , gene
The structure of the Escherichia coli ribosomal protein L25 has been determined to an r.m.s. displacement of backbone heavy atoms of 0.62 ± 0.14 Å by multi‐dimensional heteronuclear NMR spectroscopy on protein samples uniformly labeled with 15 N or 15 N/ 13 C. L25 shows a new topology for RNA‐binding proteins consisting of a six‐stranded β‐barrel and two α‐helices. A putative RNA‐binding surface for L25 has been obtained by comparison of backbone 15 N chemical shifts for L25 with and without a bound cognate RNA containing the eubacterial E‐loop that is the site for binding of L25 to 5S ribosomal RNA. Sequence comparisons with related proteins, including the general stress protein, CTC, show that the residues involved in RNA binding are highly conserved, thereby providing further confirmation of the binding surface. Tertiary structure comparisons indicate that the six‐stranded β‐barrels of L25 and of the tRNA anticodon‐binding domain of glutaminyl‐tRNA synthetase are similar.