1ZHI

Complex of the S. cerevisiae Orc1 and Sir1 interacting domains

Summary for 1ZHI

• Entry DOI: 10.2210/pdb1zhi/pdb
• Related: 1M4Z 1Z1A
• Descriptor: Origin recognition complex subunit 1, Regulatory protein SIR1 (3 entities in total)
• Functional Keywords: protein complex, bah domain, oir domain, transcription-replication complex, transcription/replication
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P54784 P21691
• Total number of polymer chains: 2
• Total formula weight: 42261.46

Authors

Hou, Z.,Bernstein, D.A.,Fox, C.A.,Keck, J.L. (deposition date: 2005-04-25, release date: 2005-06-07, Last modification date: 2024-02-14)

Primary citation

Hou, 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

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)