Understanding Cysteine Chemistry Using Conventional and Serial X-Ray Protein Crystallography.

ABSTRACT: Proteins that use cysteine residues for catalysis or regulation are widely distributed and intensively studied, with many biomedically important examples. Enzymes where cysteine is a catalytic nucleophile typically generate covalent catalytic intermediates whose structures are important for understanding mechanism and for designing targeted inhibitors. The formation of catalytic intermediates can change enzyme conformational dynamics, sometimes activating protein motions that are important for catalytic turnover. However, these transiently populated intermediate species have been challenging to structurally characterize using traditional crystallographic approaches. This review describes the use and promise of new time-resolved serial crystallographic methods to study cysteine-dependent en

SUBMITTER: Smith N 

PROVIDER: S-EPMC9850494 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature