Disorder-to-Order Transition of an Active-Site Loop Mediates the Allosteric Activation of Sortase A.

ABSTRACT: Intrinsically disordered proteins and intrinsically disordered regions are implicated in many biological functions and associated with many diseases, but their conformational characterizations are challenging. The disordered β6/β7 loop of Staphylococcus aureus sortase A is involved in the binding of both sorting signals and calcium. Calcium binding allosterically activates the enzyme, but the detailed mechanism has been unclear. Here we adapted the replica exchange with solute tempering method to sample the conformations of the β6/β7 loop, in apo form and in three liganded forms (bound with a sorting signal or calcium or both). The extensive molecular dynamics simulations yield atomic details of the disordered-to-order transition of the loop and suggest a mechanism for allosteric activatio

SUBMITTER: Pang X 

PROVIDER: S-EPMC4624160 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature