HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rzychon, M. Articles by Bochtler, M. Search for Related Content PubMed PubMed Citation Articles by Rzychon, M. Articles by Bochtler, M. Social Bookmarking                   What's this?

Staphostatins resemble lipocalins, not cystatins in fold

¹ International Institute of Molecular and Cell Biology, 02109 Warsaw, Poland
² Max-Planck-Institute for Molecular Cell Biology and Genetics, 01309 Dresden, Germany
³ Faculty of Biotechnology, Jagiellonian University, 30387 Kraków, Poland
⁴ Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA

Reprint requests to: Matthias Bochtler, International Institute of Molecular and Cell Biology, ul. Trojdena 4, 02109 Warsaw, Poland; e-mail: MBochtler{at}iimcb.gov.pl; fax: 048-22-6685288.

Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Here, we present the 1.4 Å crystal structure of staphostatin B and show that the fold can be described as a fully closed, highly sheared eight-stranded ß-barrel. Thus, staphostatin B is related to ß-barrel domains that are involved in the inhibition or regulation of proteases of various catalytic types and to the superfamily of lipocalins/cytosolic fatty acid binding proteins. Unexpectedly for a cysteine protease inhibitor, staphostatin B is not significantly similar to cystatins.

Keywords: ß-barrel; cysteine protease inhibitor; SspC; staphostatin

Abbreviations: GST, glutathione-S-transferase

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. Filipek, J. Potempa, and M. Bochtler A Comparison of Staphostatin B with Standard Mechanism Serine Protease Inhibitors J. Biol. Chem., April 15, 2005; 280(15): 14669 - 14674. [Abstract] [Full Text] [PDF]

				L. Shaw, E. Golonka, J. Potempa, and S. J. Foster The role and regulation of the extracellular proteases of Staphylococcus aureus Microbiology, January 1, 2004; 150(1): 217 - 228. [Abstract] [Full Text] [PDF]