4BK0
Crystal structure of the KIX domain of human RECQL5 (domain-swapped dimer)
Summary for 4BK0
| Entry DOI | 10.2210/pdb4bk0/pdb |
| EMDB information | 2367 |
| Descriptor | ATP-DEPENDENT DNA HELICASE Q5, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | transcription, dna helicase, transcriptional repression |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 25252.74 |
| Authors | Kassube, S.A.,Jinek, M.,Fang, J.,Tsutakawa, S.,Nogales, E. (deposition date: 2013-04-21, release date: 2013-06-12, Last modification date: 2024-05-08) |
| Primary citation | Kassube, S.A.,Jinek, M.,Fang, J.,Tsutakawa, S.,Nogales, E. Structural Mimicry in Transcription Regulation of Human RNA Polymerase II by the DNA Helicase Recql5 Nat.Struct.Mol.Biol., 20:892-, 2013 Cited by PubMed Abstract: RECQL5 is a member of the highly conserved RecQ family of DNA helicases involved in DNA repair. RECQL5 interacts with RNA polymerase II (Pol II) and inhibits transcription of protein-encoding genes by an unknown mechanism. We show that RECQL5 contacts the Rpb1 jaw domain of Pol II at a site that overlaps with the binding site for the transcription elongation factor TFIIS. Our cryo-EM structure of elongating Pol II arrested in complex with RECQL5 shows that the RECQL5 helicase domain is positioned to sterically block elongation. The crystal structure of the RECQL5 KIX domain reveals similarities with TFIIS, and binding of RECQL5 to Pol II interferes with the ability of TFIIS to promote transcriptional read-through in vitro. Together, our findings reveal a dual mode of transcriptional repression by RECQL5 that includes structural mimicry of the Pol II-TFIIS interaction. PubMed: 23748380DOI: 10.1038/NSMB.2596 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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