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6SN1

Crystal structure of the human INTS13-INTS14 complex

Summary for 6SN1
Entry DOI10.2210/pdb6sn1/pdb
DescriptorIntegrator complex subunit 13, Integrator complex subunit 14, SULFATE ION, ... (4 entities in total)
Functional Keywordsintegrator, interlocked chains, vwa, pseudosymmetrical heterodimer, rna binding protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight144172.24
Authors
Jonas, S.,Sabath, K.,Staeubli, M.L. (deposition date: 2019-08-23, release date: 2020-07-22, Last modification date: 2024-05-15)
Primary citationSabath, K.,Staubli, M.L.,Marti, S.,Leitner, A.,Moes, M.,Jonas, S.
INTS10-INTS13-INTS14 form a functional module of Integrator that binds nucleic acids and the cleavage module.
Nat Commun, 11:3422-3422, 2020
Cited by
PubMed Abstract: The Integrator complex processes 3'-ends of spliceosomal small nuclear RNAs (snRNAs). Furthermore, it regulates transcription of protein coding genes by terminating transcription after unstable pausing. The molecular basis for Integrator's functions remains obscure. Here, we show that INTS10, Asunder/INTS13 and INTS14 form a separable, functional Integrator module. The structure of INTS13-INTS14 reveals a strongly entwined complex with a unique chain interlink. Unexpected structural homology to the Ku70-Ku80 DNA repair complex suggests nucleic acid affinity. Indeed, the module displays affinity for DNA and RNA but prefers RNA hairpins. While the module plays an accessory role in snRNA maturation, it has a stronger influence on transcription termination after pausing. Asunder/INTS13 directly binds Integrator's cleavage module via a conserved C-terminal motif that is involved in snRNA processing and required for spermatogenesis. Collectively, our data establish INTS10-INTS13-INTS14 as a nucleic acid-binding module and suggest that it brings cleavage module and target transcripts into proximity.
PubMed: 32647223
DOI: 10.1038/s41467-020-17232-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.54 Å)
Structure validation

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数据于2025-11-05公开中

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