Hydrogen-Deuterium Exchange Defines Ligand-Induced Conformational Changes to the Class III Biotin Protein Ligase from Saccharomyces cerevisiae.

ABSTRACT: Biotin protein ligase (BPL) catalyzes the covalent attachment of biotin onto biotin-dependent enzymes, where it functions as an essential cofactor. Eukaryotic BPLs are distinct due to the presence of a large N-terminal extension to the conserved catalytic domain and C-terminal cap. No high-resolution structures of a eukaryotic BPL have been solved; however, previous functional studies revealed the N-terminal extension interacts with the biotinylation substrate. Mass spectrometry (MS) and complementary techniques were utilized to investigate the structure of the yeast Saccharomyces cerevisiae BPL (ScBPL). Lower resolution techniques suggested holo-ScBPL had a more compact structure and sampled fewer conformational states. In addition, solution-phase and a charge state dependent gas-phase st

SUBMITTER: Sternicki LM 

PROVIDER: S-EPMC12582158 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature