3CZ7

Molecular Basis for the Autoregulation of the Protein Acetyl Transferase Rtt109

Summary for 3CZ7

• Entry DOI: 10.2210/pdb3cz7/pdb
• Descriptor: Regulator of Ty1 transposition protein 109, ACETYL COENZYME *A (3 entities in total)
• Functional Keywords: chromatin stability, replication
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus : Q07794
• Total number of polymer chains: 1
• Total formula weight: 42991.04

Authors

Hoelz, A.,Stavropoulos, P. (deposition date: 2008-04-28, release date: 2008-09-09, Last modification date: 2024-11-13)

Primary citation

Stavropoulos, P.,Nagy, V.,Blobel, G.,Hoelz, A.
Molecular basis for the autoregulation of the protein acetyl transferase Rtt109
Proc.Natl.Acad.Sci.Usa, 105:12236-12241, 2008

PubMed Abstract: Rtt109 is a protein acetyltransferase (PAT) that is responsible for the acetylation of lysine-56 of histone 3 (H3K56) in yeast. H3K56 acetylation has been implicated in the weakening of the interaction between the histone core and the surrounding DNA in the nucleosomal particle. Rtt109, in cooperation with various histone chaperones, promotes genomic stability and is required for resistance to DNA damaging agents. Here, we present the crystal structure of Rtt109 in complex with acetyl-CoA at a 2.0-A resolution. Rtt109 consists of a core PAT domain, which binds the acetyl-CoA cofactor. A second domain, the activation domain, is tightly associated with the PAT domain. Autoacetylation of lysine-290 within the activation domain is required for stabilizing the interaction between the two domains and is essential for catalysis. Biochemical analysis demonstrates the requirement of a loop within the PAT domain for the binding of the histone chaperone Vps75, and mutational analysis identifies key residues for catalysis. We propose a model in which the autoacetylation of Rtt109 is crucial for the regulation of its catalytic activity.

PubMed: 18719104
DOI: 10.1073/pnas.0805813105

Experimental method

X-RAY DIFFRACTION (2 Å)