Estimating conformational heterogeneity of tryptophan synthase with a template-based Alphafold2 approach.

ABSTRACT: The three-dimensional structure of the enzymes provides very relevant information on the arrangement of the catalytic machinery and structural elements gating the active site pocket. The recent success of the neural network Alphafold2 in predicting the folded structure of proteins from the primary sequence with high levels of accuracy has revolutionized the protein design field. However, the application of Alphafold2 for understanding and engineering function directly from the obtained single static picture is not straightforward. Indeed, understanding enzymatic function requires the exploration of the ensemble of thermally accessible conformations that enzymes adopt in solution. In the present study, we evaluate the potential of Alphafold2 in assessing the effect of the mutations on the c

SUBMITTER: Casadevall G 

PROVIDER: S-EPMC9601780 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature