7adc

Transcription termination intermediate complex 3 delta NusG

spinqualitylabelsall models 7adc, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7adc is a 15 chain structure with sequence from Escherichia coli and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4Å Ligands: ADP, BEF, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RHO_ECOLI Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884] Publication Abstract from PubMed Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) rho on a pathway to terminating NusA/NusG-modified elongation complexes. An open rho ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the rho ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping rho subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that rho, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state. Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho.,Said N, Hilal T, Sunday ND, Khatri A, Burger J, Mielke T, Belogurov GA, Loll B, Sen R, Artsimovitch I, Wahl MC Science. 2021 Jan 1;371(6524):eabd1673. doi: 10.1126/science.abd1673. Epub 2020 , Nov 26. PMID:33243850 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase 3D structures RNA polymerase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA