Crystallographic and kinetic evidence of allostery in a trypsin-like protease.

ABSTRACT: Protein allostery is based on the existence of multiple conformations in equilibrium linked to distinct functional properties. Although evidence of allosteric transitions is relatively easy to identify by functional studies, structural detection of a pre-existing equilibrium between alternative conformations remains challenging even for textbook examples of allosteric proteins. Kinetic studies show that the trypsin-like protease thrombin exists in equilibrium between two conformations where the active site is either collapsed (E*) or accessible to substrate (E). However, structural demonstration that the two conformations exist in the same enzyme construct free of ligands has remained elusive. Here we report the crystal structure of the thrombin mutant N143P in the E form, which complement

SUBMITTER: Niu W 

PROVIDER: S-EPMC3214630 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature