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Journal of Biochemistry Advance Access originally published online on July 23, 2007
Journal of Biochemistry 2007 142(2):131-134; doi:10.1093/jb/mvm131
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© 2007 The Japanese Biochemical Society.

Rapid Communication

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

Makoto Nakakido, Yoshikazu Tanaka and Kouhei Tsumoto*

Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan

*To whom correspondence should be addressed. Tel: +81-4-7136-3600, Fax: +81-4-7136-3601, E-mail: tsumoto{at}k.u-tokyo.ac.jp

Received May 17, 2007; Accepted June 14, 2007


  Abstract

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.

Key Words: CD spectrum, elastin-binding protein of Staphylococcus aureus (EbpS), membrane-mimetic condition, secondary structure, structural change

Abbreviations: DSC, differential scanning calorimetry; EbpS, elastin-binding protein of Staphylococcus aureus; ECM, extracellular matrix; MSCRAMMs, microbial surface components recognizing adhesive matrix molecules; TFE, 2,2,2-trifluoroethanol


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