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Nominated as an outstanding Ph.D. thesis by the University of Pennsylvania, USA
Provides the reader with comprehensive and detailed structural and mechanistic insights into the NAT family of enzymes
The work presented here is the product of an international research collaboration
Glen Liszczak’s thesis provides readers with a detailed investigation into the molecular basis for protein acetylation by N-amino terminal acetyltransferase (NAT) enzymes. As part of the study, Liszczak describes how he determined the X-ray crystal structure of the N-Met_Val- specific human Naa50p NAT bound to a substrate peptide fragment and cofactor. Together with mutational and enzymatic experiments, this work reveals the molecular basis for N-amino specific acetylation and substrate specificity by NAT enzymes, how an auxiliary subunit alters the active site of a NAT catalytic subunit and how NAT enzymes evolve. Prior to Liszczak's thesis work, the molecular basis for NAT function was unknown. Therefore, these studies have important implications for understanding the activity ofthe NAT enzymes, for how regulatory subunits modulate the activity of the broader family of protein acetyltransferases, and for developing NAT-specific small molecule inhibitors for therapy.
Amino Terminal Acetylation: It's Not Your Average Birthmark.- Structure of the Ternary Naa50p Amino-terminal Acetyltransferase Complex Reveals the Molecular Basis for Substrate-specific Acetylation.- The Molecular Basis for Amino-terminal Acetylation by the NatA Complex.- Implications for the Evolution of Eukaryotic Amino-terminal Acetyltransferase Enzymes from the Structure of an Archaeal Orthologue.