The N-terminal domain of elastin-binding protein of Staphylococcus aureus changes its secondary structure in a membrane-mimetic environment.

Elastin-binding protein of Staphylococcus aureus (EbpS) has been identified as an adhesin that can bind to soluble elastin or tropoelastin. However, the structure and exact function of EbpS remain to be elucidated. To gain insight into the molecular characteristics of EbpS, we investigated the physical properties of its N-terminal extracellular domain in various environments. CD spectroscopy showed that this protein was soluble and unstructured under aqueous conditions. Non-native secondary structures, however, were induced by several alcohols that provided membrane-mimetic environments. These changes may have some correlation with the function of this protein.