 |
PDBsum entry 1b75
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
RNA binding protein
|
PDB id
|
|
|
|
1b75
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The nmr structure of escherichia coli ribosomal protein l25 shows homology to general stress proteins and glutaminyl-Trna synthetases.
|
|
|
Authors
|
|
M.Stoldt,
J.Wöhnert,
M.Görlach,
L.R.Brown.
|
|
|
Ref.
|
|
Embo J, 1998,
17,
6377-6384.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
