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.
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| 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Luo X, Hsiao HH, Bubunenko M, Weber G, Court DL, Gottesman ME, Urlaub H, Wahl MC. Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex. Mol Cell. 2008 Dec 26;32(6):791-802. PMID:19111659 doi:10.1016/j.molcel.2008.10.028
