期刊
EMBO JOURNAL
卷 19, 期 5, 页码 807-818出版社
WILEY
DOI: 10.1093/emboj/19.5.807
关键词
feedback regulation of transcription and; translation; ribosomal protein L4; rRNA and mRNA-binding proteins; S10 operon; X-ray crystallography
Ribosomal protein L4 resides near the peptidyl transferase center of the bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation. Escherichia coli L4 is also an autogenous feedback regulator of transcription and translation of the 11 gene S10 operon, The crystal structure of L4 from Thermotoga maritima at 1.7 Angstrom resolution shows the protein with an alternating alp fold and a large disordered loop region. Two separate binding sites for RNA are discernible. The N-terminal site, responsible for binding to rRNA, consists of the disordered loop with flanking a-helices, The C-terminal site, a prime candidate for the interaction with the leader sequence of the S10 mRNA, involves two non-consecutive cr-helices. The structure also suggests a C-terminal protein-binding interface, through which L4 could be interacting with protein components of the transcriptional and/or translational machineries.
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