Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1Z1A

S. cerevisiae Sir1 ORC-interaction domain

Summary for 1Z1A
Entry DOI10.2210/pdb1z1a/pdb
Related1ZHI
DescriptorRegulatory protein SIR1 (2 entities in total)
Functional Keywordsnovel fold, transcription
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationNucleus: P21691
Total number of polymer chains2
Total formula weight33692.20
Authors
Hou, Z.,Bernstein, D.A.,Fox, C.A.,Keck, J.L. (deposition date: 2005-03-03, release date: 2005-06-07, Last modification date: 2024-10-30)
Primary citationHou, Z.,Bernstein, D.A.,Fox, C.A.,Keck, J.L.
Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing.
Proc.Natl.Acad.Sci.Usa, 102:8489-8494, 2005
Cited by
PubMed Abstract: The Sir1 protein plays a key role in establishing a silent chromatin structure at the cryptic mating-type loci HMR and HML in Saccharomyces cerevisiae by interacting with the bromo-adjacent homology (BAH) domain of the Orc1p subunit of the origin recognition complex (ORC). Here, we present the high-resolution crystal structures of the ORC interaction region (OIR) of Sir1p and that of the complex formed between the OIR and BAH domains. Amino acids within the OIR previously shown to be required for a Sir1p/ORC interaction are presented on a conserved, convex surface that forms a complementary interface with a concave region of the Orc1 BAH domain that is critical for transcriptional silencing. The OIR/BAH interaction surface comprises a network of hydrophobic and polar/ionic interactions between discrete structural modules in each protein and involves several residues that were not implicated in previous studies. These data provide important structural insights into a protein-protein interaction critical for the formation of a specialized chromatin domain within eukaryotic chromosomes.
PubMed: 15932939
DOI: 10.1073/pnas.0503525102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon