The Staphylococcus aureus extracellular adherence protein (Eap) adopts an elongated but structured conformation in solution.

ABSTRACT: The extracellular adherence protein (Eap) of Staphylococcus aureus participates in a wide range of protein-protein interactions that facilitate the initiation and dissemination of Staphylococcal disease. In this report, we describe the use of a multidisciplinary approach to characterize the solution structure of full-length Eap. In contrast to previous reports suggesting that a six-domain isoform of Eap undergoes multimerization, sedimentation equilibrium analytical ultracentrifugation data revealed that a four-domain isoform of Eap is a monomer in solution. In vitro proteolysis and solution small angle X-ray scattering studies both indicate that Eap adopts an extended conformation in solution, where the linkers connecting sequential EAP modules are solvent exposed. Construction of a low-r

SUBMITTER: Hammel M 

PROVIDER: S-EPMC2222813 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature