Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for λN-dependent processive transcription antitermination.
Journal, issue, pages	Nat Microbiol, Vol. 2, Page 17062, Year 2017
Publish date	Apr 28, 2017
Authors	Nelly Said / Ferdinand Krupp / Ekaterina Anedchenko / Karine F Santos / Olexandr Dybkov / Yong-Heng Huang / Chung-Tien Lee / Bernhard Loll / Elmar Behrmann / Jörg Bürger / Thorsten Mielke / Justus Loerke / Henning Urlaub / Christian M T Spahn / Gert Weber / Markus C Wahl /
PubMed Abstract	λN-mediated processive antitermination constitutes a paradigmatic transcription regulatory event, during which phage protein λN, host factors NusA, NusB, NusE and NusG, and an RNA nut site render ...λN-mediated processive antitermination constitutes a paradigmatic transcription regulatory event, during which phage protein λN, host factors NusA, NusB, NusE and NusG, and an RNA nut site render elongating RNA polymerase termination-resistant. The structural basis of the process has so far remained elusive. Here we describe a crystal structure of a λN-NusA-NusB-NusE-nut site complex and an electron cryo-microscopic structure of a complete transcription antitermination complex, comprising RNA polymerase, DNA, nut site RNA, all Nus factors and λN, validated by crosslinking/mass spectrometry. Due to intrinsic disorder, λN can act as a multiprotein/RNA interaction hub, which, together with nut site RNA, arranges NusA, NusB and NusE into a triangular complex. This complex docks via the NusA N-terminal domain and the λN C-terminus next to the RNA exit channel on RNA polymerase. Based on the structures, comparative crosslinking analyses and structure-guided mutagenesis, we hypothesize that λN mounts a multipronged strategy to reprogram the transcriptional machinery, which may include (1) the λN C terminus clamping the RNA exit channel, thus stabilizing the DNA:RNA hybrid; (2) repositioning of NusA and RNAP elements, thus redirecting nascent RNA and sequestering the upstream branch of a terminator hairpin; and (3) hindering RNA engagement of termination factor ρ and/or obstructing ρ translocation on the transcript.
External links	Nat Microbiol / PubMed:28452979
Methods	EM (single particle) / X-ray diffraction
Resolution	2.143 - 9.8 Å
Structure data	3561 5ms0 EMDB-3561: map of the RNA polymerase lambda-based antitermination complex solved by cryo-EM PDB-5ms0: pseudo-atomic model of the RNA polymerase lambda-based antitermination complex solved by cryo-EM Method: EM (single particle) / Resolution: 9.8 Å PDB-5lm7: Crystal structure of the lambda N-Nus factor complex Method: X-RAY DIFFRACTION / Resolution: 3.35 Å PDB-5lm9: Structure of E. coli NusA Method: X-RAY DIFFRACTION / Resolution: 2.143 Å
Chemicals	ChemComp-SO4: SULFATE ION ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-ZN: Unknown entry
Source	escherichia coli (E. coli) escherichia phage lambda (virus) escherichia coli k-12 (bacteria) escherichia coli o157:h7 (bacteria) escherichia coli o45:k1 (strain s88 / expec) (bacteria) enterobacteria phage lambda (virus)
Keywords	TRANSCRIPTION / Transcription regulation antitermination Nus proteins Phage lambda N protein / Transcription factor / Antitermination Termination / Nus proteins / TRANSCRIPTION/DNA/RNA / DNA-DEPENDENT RNA POLYMERASE / BACTERIAL TRANSCRIPTION / TERNARY ELONGATION COMPLEX / ANTITERMINATION / TRANSCRIPTION-DNA-RNA complex