1DMG

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4

Summary for 1DMG

• Entry DOI: 10.2210/pdb1dmg/pdb
• Descriptor: RIBOSOMAL PROTEIN L4, CITRIC ACID (3 entities in total)
• Functional Keywords: alpha-beta, ribosomal protein, l4, ribosome, rna, s10 operon, gene regulation
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 25883.02

Authors

Worbs, M.,Huber, R.,Wahl, M.C. (deposition date: 1999-12-14, release date: 2000-12-18, Last modification date: 2024-02-07)

Primary citation

Worbs, M.,Huber, R.,Wahl, M.C.
Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon.
EMBO J., 19:807-818, 2000

PubMed Abstract: 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.

PubMed: 10698923
DOI: 10.1093/emboj/19.5.807

Experimental method

X-RAY DIFFRACTION (1.7 Å)