Skip Navigation



Journal of Biochemistry Advance Access published online on July 23, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm131
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow Supplementary data
Right arrow All Versions of this Article:
142/2/131    most recent
mvm131v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Nakakido, M.
Right arrow Articles by Tsumoto, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakakido, M.
Right arrow Articles by Tsumoto, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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. Kouhei Tsumoto, 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 chang


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.