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8R6R

Mycobacterium smegnatis RNA polymerase RP2-like transcription initiation complex with SigmaA, RbpA and open promoter DNA

Summary for 8R6R
Entry DOI10.2210/pdb8r6r/pdb
Related8Q3I
EMDB information18959
DescriptorDNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
Functional Keywordsheld, rna polymerase, transcription initiation, mycobacteria, transcription, rifampicin resistance
Biological sourceMycolicibacterium smegmatis MC2 155
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Total number of polymer chains9
Total formula weight458579.95
Authors
Koval, T.,Krasny, L.,Dohnalek, J.,Kouba, T. (deposition date: 2023-11-22, release date: 2024-10-02, Last modification date: 2024-12-11)
Primary citationKoval, T.,Borah, N.,Sudzinova, P.,Brezovska, B.,Sanderova, H.,Vankova Hausnerova, V.,Krenkova, A.,Hubalek, M.,Trundova, M.,Adamkova, K.,Duskova, J.,Schwarz, M.,Wiedermannova, J.,Dohnalek, J.,Krasny, L.,Kouba, T.
Mycobacterial HelD connects RNA polymerase recycling with transcription initiation.
Nat Commun, 15:8740-8740, 2024
Cited by
PubMed Abstract: Mycobacterial HelD is a transcription factor that recycles stalled RNAP by dissociating it from nucleic acids and, if present, from the antibiotic rifampicin. The rescued RNAP, however, must disengage from HelD to participate in subsequent rounds of transcription. The mechanism of release is unknown. We show that HelD from Mycobacterium smegmatis forms a complex with RNAP associated with the primary sigma factor σ and transcription factor RbpA but not CarD. We solve several structures of RNAP-σ-RbpA-HelD without and with promoter DNA. These snapshots capture HelD during transcription initiation, describing mechanistic aspects of HelD release from RNAP and its protective effect against rifampicin. Biochemical evidence supports these findings, defines the role of ATP binding and hydrolysis by HelD in the process, and confirms the rifampicin-protective effect of HelD. Collectively, these results show that when HelD is present during transcription initiation, the process is protected from rifampicin until the last possible moment.
PubMed: 39384756
DOI: 10.1038/s41467-024-52891-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.89 Å)
Structure validation

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