The Role of Rigid Residues in Modulating TEM-1 β-Lactamase Function and Thermostability.

ABSTRACT: The relationship between protein motions (i.e., dynamics) and enzymatic function has begun to be explored in β-lactamases as a way to advance our understanding of these proteins. In a recent study, we analyzed the dynamic profiles of TEM-1 (a ubiquitous class A β-lactamase) and several ancestrally reconstructed homologues. A chief finding of this work was that rigid residues that were allosterically coupled to the active site appeared to have profound effects on enzyme function, even when separated from the active site by many angstroms. In the present work, our aim was to further explore the implications of protein dynamics on β-lactamase function by altering the dynamic profile of TEM-1 using computational protein design methods. The Rosetta software suite was used to mutate amino acids

SUBMITTER: Kolbaba-Kartchner B 

PROVIDER: S-EPMC7999226 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature