Role of cis-trans proline isomerization in the function of pathogenic enterobacterial Periplasmic Binding Proteins.

ABSTRACT: Periplasmic Binding Proteins (PBPs) trap nutrients for their internalization into bacteria by ABC transporters. Ligand binding triggers PBP closure by bringing its two domains together like a Venus flytrap. The atomic determinants that control PBP opening and closure for nutrient capture and release are not known, although it is proposed that opening and ligand release occur while in contact with the ABC transporter for concurrent substrate translocation. In this paper we evaluated the effect of the isomerization of a conserved proline, located near the binding site, on the propensity of PBPs to open and close. ArgT/LAO from Salmonella typhimurium and HisJ from Escherichia coli were studied through molecular mechanics at two different temperatures: 300 and 323 K. Eight microseconds were si

SUBMITTER: Cortes-Hernandez P 

PROVIDER: S-EPMC5708682 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature