Analyzing In Silico the Relationship Between the Activation of the Edema Factor and Its Interaction With Calmodulin.

ABSTRACT: Molecular dynamics (MD) simulations have been recorded on the complex between the edema factor (EF) of Bacilllus anthracis and calmodulin (CaM), starting from a structure with the orthosteric inhibitor adefovir bound in the EF catalytic site. The starting structure has been destabilized by alternately suppressing different co-factors, such as adefovir ligand or ions, revealing several long-distance correlations between the conformation of CaM, the geometry of the CaM/EF interface, the enzymatic site and the overall organization of the complex. An allosteric communication between CaM/EF interface and the EF catalytic site, highlighted by these correlations, was confirmed by several bioinformatics approaches from the literature. A network of hydrogen bonds and stacking interactions ex

SUBMITTER: Pitard I 

PROVIDER: S-EPMC7746812 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature