Direct observation of T4 lysozyme hinge-bending motion by fluorescence correlation spectroscopy.

ABSTRACT: Bacteriophage T4 Lysozyme (T4L) catalyzes the hydrolysis of the peptidoglycan layer of the bacterial cell wall late in the infection cycle. It has long been postulated that equilibrium dynamics enable substrate access to the active site located at the interface between the N- and C-terminal domains. Crystal structures of WT-T4L and point mutants captured a range of conformations that differ by the hinge-bending angle between the two domains. Evidence of equilibrium between open and closed conformations in solution was gleaned from distance measurements between the two domains but the nature of the equilibrium and the timescale of the underlying motion have not been investigated. Here, we used fluorescence fluctuation spectroscopy to directly detect T4L equilibrium conformational fluctuatio

SUBMITTER: Yirdaw RB 

PROVIDER: S-EPMC3471472 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature