3d3c | pdb_00003d3c

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

spinqualitylabelsall models 3d3c, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3d3c is a 6 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3d3b Gene: nusB, ssyB, b0416, JW0406 (ECOLI), rpsJ, nusE, b3321, JW3283 (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [NUSB_ECOLI] One of the proteins essential for the formation of the RNA polymerase antitermination complex in the presence of lambda phage N protein. However, it is involved in the transcription termination process at certain sites during normal bacterial growth. Binds to the BoxA RNA motif. [RS10_ECOLI] Involved in the binding of tRNA to the ribosomes.[HAMAP-Rule:MF_00508] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.,Luo X, Hsiao HH, Bubunenko M, Weber G, Court DL, Gottesman ME, Urlaub H, Wahl MC Mol Cell. 2008 Dec 26;32(6):791-802. PMID:19111659 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein S10

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