1RQS

NMR structure of C-terminal domain of ribosomal protein L7 from E.coli

1RQS の概要

• エントリーDOI: 10.2210/pdb1rqs/pdb
• 関連するPDBエントリー: 1CTF 1DD3 1DD4 1RQT 1RQU 1RQV
• 分子名称: 50S ribosomal protein L7/L12 (1 entity in total)
• 機能のキーワード: protein l7/l12, ribosome
• 由来する生物種: Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, Shigella flexneri (, , ,)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7573.64

構造登録者

Bocharov, E.V.,Sobol, A.G.,Pavlov, K.V.,Korzhnev, D.M.,Jaravine, V.A.,Gudkov, A.T.,Arseniev, A.S. (登録日: 2003-12-07, 公開日: 2004-03-02, 最終更新日: 2024-05-22)

主引用文献

Bocharov, E.V.,Sobol, A.G.,Pavlov, K.V.,Korzhnev, D.M.,Jaravine, V.A.,Gudkov, A.T.,Arseniev, A.S.
From structure and dynamics of protein L7/L12 to molecular switching in ribosome.
J.Biol.Chem., 279:17697-17706, 2004

PubMed Abstract: Based on the (1)H-(15)N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked via flexible hinge regions. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel alpha-alpha-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact alpha/beta-fold. There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region. Combining structural data for the ribosomal protein L7/L12 from NMR spectroscopy and x-ray crystallography, it was suggested that its hinge region acts as a molecular switch, initiating "ratchet-like" motions of the L7/L12 stalk with respect to the ribosomal surface in response to elongation factor binding and GTP hydrolysis. This hypothesis allows an explanation of events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome.

PubMed: 14960595
DOI: 10.1074/jbc.M313384200

実験手法

SOLUTION NMR