4S20
Structural basis for transcription reactivation by RapA
Summary for 4S20
| Entry DOI | 10.2210/pdb4s20/pdb |
| Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total) |
| Functional Keywords | dna-directed rna polymerase, transcription transferase, dna translocase, atpase, transferase-dna-rna complex, transferase/dna/rna |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 16 |
| Total formula weight | 1017744.46 |
| Authors | Liu, B.,Zuo, Y.,Steitz, T.A. (deposition date: 2015-01-16, release date: 2015-02-04, Last modification date: 2024-11-20) |
| Primary citation | Liu, B.,Zuo, Y.,Steitz, T.A. Structural basis for transcription reactivation by RapA. Proc.Natl.Acad.Sci.USA, 112:2006-2010, 2015 Cited by PubMed Abstract: RNA polymerase (RNAP) loses activity during transcription as it stalls at various inactive states due to erratic translocation. Reactivation of these stalled RNAPs is essential for efficient RNA synthesis. Here we report a 4.7-Å resolution crystal structure of the Escherichia coli RNAP core enzyme in complex with ATPase RapA that is involved in reactivating stalled RNAPs. The structure reveals that RapA binds at the RNA exit channel of the RNAP and makes the channel unable to accommodate the formation of an RNA hairpin. The orientation of RapA on the RNAP core complex suggests that RapA uses its ATPase activity to propel backward translocation of RNAP along the DNA template in an elongation complex. This structure provides insights into the reactivation of stalled RNA polymerases and helps support ATP-driven backward translocation as a general mechanism for transcriptional regulation. PubMed: 25646438DOI: 10.1073/pnas.1417152112 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.7 Å) |
Structure validation
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