6rr0

Crystal structure of the Sir4 H-BRCT domain in complex with Ubp10 pT123 peptide

spinqualitylabelsall models 6rr0, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rr0 is a 14 chain structure with sequence from Saccharomyces cerevisiae and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.18Å Ligands: CL, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SIR4_YEAST The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. Publication Abstract from PubMed In Saccharomyces cerevisiae, the silent information regulator (SIR) proteins Sir2/3/4 form a complex that suppresses transcription in subtelomeric regions and at the homothallic mating-type (HM) loci. Here, we identify a non-canonical BRCA1 C-terminal domain (H-BRCT) in Sir4, which is responsible for tethering telomeres to the nuclear periphery. We show that Sir4 H-BRCT and the closely related Dbf4 H-BRCT serve as selective phospho-epitope recognition domains that bind to a variety of phosphorylated target peptides. We present detailed structural information about the binding mode of established Sir4 interactors (Esc1, Ty5, Ubp10) and identify several novel interactors of Sir4 H-BRCT, including the E3 ubiquitin ligase Tom1. Based on these findings, we propose a phospho-peptide consensus motif for interaction with Sir4 H-BRCT and Dbf4 H-BRCT. Ablation of the Sir4 H-BRCT phospho-peptide interaction disrupts SIR-mediated repression and perinuclear localization. In conclusion, the Sir4 H-BRCT domain serves as a hub for recruitment of phosphorylated target proteins to heterochromatin to properly regulate silencing and nuclear order. The Sir4 H-BRCT domain interacts with phospho-proteins to sequester and repress yeast heterochromatin.,Deshpande I, Keusch JJ, Challa K, Iesmantavicius V, Gasser SM, Gut H EMBO J. 2019 Oct 15;38(20):e101744. doi: 10.15252/embj.2019101744. Epub 2019 Sep , 12. PMID:31515872 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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