1B75

SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L25 FROM ESCHERICHIA COLI

Summary for 1B75

• Entry DOI: 10.2210/pdb1b75/pdb
• NMR Information: BMRB: 4395
• Descriptor: PROTEIN (50S RIBOSOMAL PROTEIN L25) (1 entity in total)
• Functional Keywords: ribosomal protein, rna-binding protein, rna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 10713.47

Authors

Stoldt, M.,Woehnert, J.,Goerlach, M.,Brown, L.R. (deposition date: 1999-01-27, release date: 2000-01-26, Last modification date: 2023-12-27)

Primary citation

Stoldt, M.,Wohnert, J.,Gorlach, M.,Brown, L.R.
The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
EMBO J., 17:6377-6384, 1998

PubMed Abstract: 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 A by multi-dimensional heteronuclear NMR spectroscopy on protein samples uniformly labeled with 15N or 15N/13C. L25 shows a new topology for RNA-binding proteins consisting of a six-stranded beta-barrel and two alpha-helices. A putative RNA-binding surface for L25 has been obtained by comparison of backbone 15N 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 beta-barrels of L25 and of the tRNA anticodon-binding domain of glutaminyl-tRNA synthetase are similar.

PubMed: 9799245
DOI: 10.1093/emboj/17.21.6377

Experimental method

SOLUTION NMR