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

Makoto Nakakido, Yoshikazu Tanaka, Kouhei Tsumoto

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)131-134
Number of pages4
JournalJournal of biochemistry
Volume142
Issue number2
DOIs
Publication statusPublished - 2007 Aug 1
Externally publishedYes

Keywords

  • CD spectrum
  • Elastin-binding protein of Staphylococcus aureus (EbpS)
  • Membrane-mimetic condition
  • Secondary structure
  • Structural change

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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