6jny

Crystal structure of bacteriophage 21 Q protein

spinqualitylabelsall models 6jny, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jny is a 2 chain structure with sequence from Enterobacteria phage SfI. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.451Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1FPN0_9CAUD Publication Abstract from PubMed Bacteriophage Q protein engages sigma-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for sigma-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (Q(I) and Q(II)) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, Q(I) forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well. Structural basis of Q-dependent transcription antitermination.,Shi J, Gao X, Tian T, Yu Z, Gao B, Wen A, You L, Chang S, Zhang X, Zhang Y, Feng Y Nat Commun. 2019 Jul 2;10(1):2925. doi: 10.1038/s41467-019-10958-8. PMID:31266960 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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