6IB8
Structure of a complex of SuhB and NusA AR2 domain
Summary for 6IB8
| Entry DOI | 10.2210/pdb6ib8/pdb |
| Descriptor | Inositol-1-monophosphatase, Transcription termination/antitermination protein NusA, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | suhb, nusa ar2 domain, antitermiantion, transcription |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 3 |
| Total formula weight | 68240.78 |
| Authors | Huang, Y.H.,Loll, B.,Wahl, M.C. (deposition date: 2018-11-29, release date: 2019-04-17, Last modification date: 2024-01-24) |
| Primary citation | Huang, Y.H.,Said, N.,Loll, B.,Wahl, M.C. Structural basis for the function of SuhB as a transcription factor in ribosomal RNA synthesis. Nucleic Acids Res., 47:6488-6503, 2019 Cited by PubMed Abstract: Ribosomal RNA synthesis in Escherichia coli involves a transcription complex, in which RNA polymerase is modified by a signal element on the transcript, Nus factors A, B, E and G, ribosomal protein S4 and inositol mono-phosphatase SuhB. This complex is resistant to ρ-dependent termination and facilitates ribosomal RNA folding, maturation and subunit assembly. The functional contributions of SuhB and their structural bases are presently unclear. We show that SuhB directly binds the RNA signal element and the C-terminal AR2 domain of NusA, and we delineate the atomic basis of the latter interaction by macromolecular crystallography. SuhB recruitment to a ribosomal RNA transcription complex depends on the RNA signal element but not on the NusA AR2 domain. SuhB in turn is required for stable integration of the NusB/E dimer into the complex. In vitro transcription assays revealed that SuhB is crucial for delaying or suppressing ρ-dependent termination, that SuhB also can reduce intrinsic termination, and that SuhB-AR2 contacts contribute to these effects. Together, our results reveal functions of SuhB during ribosomal RNA synthesis and delineate some of the underlying molecular interactions. PubMed: 31020314DOI: 10.1093/nar/gkz290 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.646 Å) |
Structure validation
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