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8R6P

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

Summary for 8R6P
Entry DOI10.2210/pdb8r6p/pdb
Related8Q3I
EMDB information18956
DescriptorDNA-directed RNA polymerase subunit alpha, ZINC ION, MAGNESIUM ION, ... (11 entities in total)
Functional Keywordsheld, rna polymerase, transcription initiation, mycobacteria, transcription, rifampicin resistance
Biological sourceMycolicibacterium smegmatis MC2 155
More
Total number of polymer chains10
Total formula weight474795.05
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 (3.16 Å)
Structure validation

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