Mevalonate 5-diphosphate mediates ATP binding to the mevalonate diphosphate decarboxylase from the bacterial pathogen Enterococcus faecalis.

ABSTRACT: The mevalonate pathway produces isopentenyl diphosphate (IPP), a building block for polyisoprenoid synthesis, and is a crucial pathway for growth of the human bacterial pathogen Enterococcus faecalis The final enzyme in this pathway, mevalonate diphosphate decarboxylase (MDD), acts on mevalonate diphosphate (MVAPP) to produce IPP while consuming ATP. This essential enzyme has been suggested as a therapeutic target for the treatment of drug-resistant bacterial infections. Here, we report functional and structural studies on the mevalonate diphosphate decarboxylase from E. faecalis (MDD_EF). The MDD_EF crystal structure in complex with ATP (MDD_EF-ATP) revealed that the phosphate-binding loop (amino acids 97-105) is not involved in ATP binding and

SUBMITTER: Chen CL 

PROVIDER: S-EPMC5766736 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature