1DMG

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4

1DMG の概要

• エントリーDOI: 10.2210/pdb1dmg/pdb
• 分子名称: RIBOSOMAL PROTEIN L4, CITRIC ACID (3 entities in total)
• 機能のキーワード: alpha-beta, ribosomal protein, l4, ribosome, rna, s10 operon, gene regulation
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25883.02

構造登録者

Worbs, M.,Huber, R.,Wahl, M.C. (登録日: 1999-12-14, 公開日: 2000-12-18, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)