6ZFB
Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer)
Summary for 6ZFB
| Entry DOI | 10.2210/pdb6zfb/pdb |
| EMDB information | 11105 |
| Descriptor | DNA-directed RNA polymerase subunit delta, RNA polymerase subunit omega, DNA-directed RNA polymerase subunit alpha, ... (7 entities in total) |
| Functional Keywords | transcription/dna/rna, dna-dependent rna polymerase, bacterial, transcription, helicase |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 14 |
| Total formula weight | 905367.71 |
| Authors | Pei, H.-P.,Hilal, T.,Huang, Y.-H.,Said, N.,Loll, B.,Wahl, M.C. (deposition date: 2020-06-17, release date: 2020-10-14, Last modification date: 2024-05-15) |
| Primary citation | Pei, H.H.,Hilal, T.,Chen, Z.A.,Huang, Y.H.,Gao, Y.,Said, N.,Loll, B.,Rappsilber, J.,Belogurov, G.A.,Artsimovitch, I.,Wahl, M.C. The delta subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling. Nat Commun, 11:6418-6418, 2020 Cited by PubMed Abstract: Cellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains elusive. In Bacillus subtilis, the RNAP δ subunit and NTPase HelD have been implicated in RNAP recycling. We structurally analyzed Bacillus subtilis RNAP-δ-HelD complexes. HelD has two long arms: a Gre cleavage factor-like coiled-coil inserts deep into the RNAP secondary channel, dismantling the active site and displacing RNA, while a unique helical protrusion inserts into the main channel, prying the β and β' subunits apart and, aided by δ, dislodging DNA. RNAP is recycled when, after releasing trapped nucleic acids, HelD dissociates from the enzyme in an ATP-dependent manner. HelD abundance during slow growth and a dimeric (RNAP-δ-HelD) structure that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzyme pools in response to cellular cues. PubMed: 33339827DOI: 10.1038/s41467-020-20159-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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