3D3B

Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.

Summary for 3D3B

• Entry DOI: 10.2210/pdb3d3b/pdb
• Related: 3D3C
• Descriptor: N utilization substance protein B, 30S ribosomal protein S10, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (4 entities in total)
• Functional Keywords: nusb, s10, nuse, nut site, phage lambda, lambdan antitermination, rrn antitermination, transcription control, rna-binding, transcription, transcription regulation, transcription termination, ribonucleoprotein, ribosomal protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 26068.11

Authors

Luo, X.,Wahl, M.C. (deposition date: 2008-05-09, release date: 2009-01-13, Last modification date: 2023-08-30)

Primary citation

Luo, X.,Hsiao, H.H.,Bubunenko, M.,Weber, G.,Court, D.L.,Gottesman, M.E.,Urlaub, H.,Wahl, M.C.
Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.
Mol.Cell, 32:791-802, 2008

PubMed Abstract: Protein S10 is a component of the 30S ribosomal subunit and participates together with NusB protein in processive transcription antitermination. The molecular mechanisms by which S10 can act as a translation or a transcription factor are not understood. We used complementation assays and recombineering to delineate regions of S10 dispensable for antitermination, and determined the crystal structure of a transcriptionally active NusB-S10 complex. In this complex, S10 adopts the same fold as in the 30S subunit and is blocked from simultaneous association with the ribosome. Mass spectrometric mapping of UV-induced crosslinks revealed that the NusB-S10 complex presents an intermolecular, composite, and contiguous binding surface for RNAs containing BoxA antitermination signals. Furthermore, S10 overproduction complemented a nusB null phenotype. These data demonstrate that S10 and NusB together form a BoxA-binding module, that NusB facilitates entry of S10 into the transcription machinery, and that S10 represents a central hub in processive antitermination.

PubMed: 19111659
DOI: 10.1016/j.molcel.2008.10.028

Experimental method

X-RAY DIFFRACTION (1.3 Å)