1RQT

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

Summary for 1RQT

• Entry DOI: 10.2210/pdb1rqt/pdb
• Related: 1CTF 1DD3 1DD4 1RQS 1RQU 1RQV
• Descriptor: 50S ribosomal protein L7/L12 (1 entity in total)
• Functional Keywords: protein l7/l12, ribosome
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 7656.85

Authors

Bocharov, E.V.,Sobol, A.G.,Pavlov, K.V.,Korzhnev, D.M.,Jaravine, V.A.,Gudkov, A.T.,Arseniev, A.S. (deposition date: 2003-12-07, release date: 2004-03-02, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR