1dmg
From Proteopedia
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CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4
Overview
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 A resolution shows the, protein with an alternating alpha/beta 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 alpha-helices. The C-terminal site, a prime candidate for, the interaction with the leader sequence of the S10 mRNA, involves two, non-consecutive alpha-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.
About this Structure
1DMG is a Single protein structure of sequence from Thermotoga maritima with CIT as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon., Worbs M, Huber R, Wahl MC, EMBO J. 2000 Mar 1;19(5):807-18. PMID:10698923
Page seeded by OCA on Tue Nov 20 13:24:36 2007
Categories: Single protein | Thermotoga maritima | Huber, R. | Wahl, M.C. | Worbs, M. | CIT | Alpha-beta | L4 | Ribosomal protein | Ribosome | Rna | S10 operon
