7BFQ

Structure of the Integrator cleavage module with extended INTS4 and rigid body docked INTS9/11 CTD

Summary for 7BFQ

• Entry DOI: 10.2210/pdb7bfq/pdb
• EMDB information: 12166
• Descriptor: Integrator complex subunit 9, Integrator complex subunit 4, Integrator complex subunit 11, ... (4 entities in total)
• Functional Keywords: nuclease, integrator, 3'-end processing, nuclear protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 271316.94

Authors

Pfleiderer, M.M.,Galej, W.P. (deposition date: 2021-01-04, release date: 2021-03-24, Last modification date: 2024-07-10)

Primary citation

Pfleiderer, M.M.,Galej, W.P.
Structure of the catalytic core of the Integrator complex.
Mol.Cell, 81:1246-, 2021

PubMed Abstract: The Integrator is a specialized 3' end-processing complex involved in cleavage and transcription termination of a subset of nascent RNA polymerase II transcripts, including small nuclear RNAs (snRNAs). We provide evidence of the modular nature of the Integrator complex by biochemically characterizing its two subcomplexes, INTS5/8 and INTS10/13/14. Using cryoelectron microscopy (cryo-EM), we determined a 3.5-Å-resolution structure of the INTS4/9/11 ternary complex, which constitutes Integrator's catalytic core. Our structure reveals the spatial organization of the catalytic nuclease INTS11, bound to its catalytically impaired homolog INTS9 via several interdependent interfaces. INTS4, a helical repeat protein, plays a key role in stabilizing nuclease domains and other components. In this assembly, all three proteins form a composite electropositive groove, suggesting a putative RNA binding path within the complex. Comparison with other 3' end-processing machineries points to distinct features and a unique architecture of the Integrator's catalytic module.

PubMed: 33548203
DOI: 10.1016/j.molcel.2021.01.005

Experimental method

ELECTRON MICROSCOPY (4.15 Å)