The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases

被引:67
作者
Stoldt, M [1 ]
Wöhnert, J [1 ]
Görlach, M [1 ]
Brown, LR [1 ]
机构
[1] Inst Mol Biotechnol EV, Abt Mol Biophys NMR Spektroskopie, D-07708 Jena, Germany
关键词
NMR spectroscopy; protein structure; ribosomal protein; ribosome; RNA binding;
D O I
10.1093/emboj/17.21.6377
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom by multidimensional heteronuclear NMR spectroscopy on protein samples uniformly labeled with N-15 or N-15/C-13. L25 shows a new topology for RNA-binding proteins consisting of a six-stranded beta-barrel and two a-helices. A putative RNA-binding surface for L25 has been obtained by comparison of backbone N-15 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.
引用
收藏
页码:6377 / 6384
页数:8
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