6vsx | pdb_00006vsx

X-ray crystal structure of the C-terminal domain of Bacillus subtilis RNA polymerase binding helicase HelD

spinqualitylabelsall models 6vsx, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vsx is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Gene: B4417_3167 ("Vibrio subtilis" Ehrenberg 1835) Activity: DNA helicase, with EC number 3.6.4.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids. Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.,Kouba T, Koval' T, Sudzinova P, Pospisil J, Brezovska B, Hnilicova J, Sanderova H, Janouskova M, Sikova M, Halada P, Sykora M, Barvik I, Novacek J, Trundova M, Duskova J, Skalova T, Chon U, Murakami KS, Dohnalek J, Krasny L Nat Commun. 2020 Dec 18;11(1):6419. doi: 10.1038/s41467-020-20158-4. PMID:33339823 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA