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

J. Biol. Chem., Vol. 280, Issue 7, 5820-5827, February 18, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/7/5820    most recent M411238200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Shouldice, S. R. Articles by Schryvers, A. B. Search for Related Content PubMed PubMed Citation Articles by Shouldice, S. R. Articles by Schryvers, A. B. Social Bookmarking                      What's this?

Novel Anion-independent Iron Coordination by Members of a Third Class of Bacterial Periplasmic Ferric Ion-binding Proteins^*

Stephen R. Shouldice, Duncan E. McRee¶, Douglas R. Dougan||, Leslie W. Tari¶, and Anthony B. Schryvers**

From the Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta T2N 4N1, Canada and ^¶ActiveSight and ^||Syrrx Inc., San Diego, California 92121

The uptake of the element iron is vital for the survival of most organisms. Numerous pathogenic Gram-negative bacteria utilize a periplasm-to-cytosol ATP-binding cassette transport pathway to transport this essential atom in to the cell. In this study, we investigated the Yersinia enterocolitica (YfuA) and Serratia marcescens (SfuA) iron-binding periplasmic proteins. We have determined the 1.8-Å structures of iron-loaded (YfuA) and iron-free (SfuA) forms of this class of proteins. Although the sequence of these proteins varies considerably from the other members of the transferrin structural superfamily, they adopt the same three-dimensional fold. The iron-loaded YfuA structure illustrates the unique nature of this new class of proteins in that they are able to octahedrally coordinate the ferric ion in the absence of a bound anion. The iron-free SfuA structure contains a bound citrate anion in the iron-binding cleft that tethers the N- and C-terminal domains of the apo protein and stabilizes the partially open structure.

Received for publication, October 1, 2004 , and in revised form, November 30, 2004.

The atomic coordinates and structure factors (codes 1XVY and 1XVX) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by Grant 49603 from the Canadian Institutes for Health Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a Studentship from University Technologies International.

^** To whom correspondence should be addressed. Tel.: 403-220-3703; Fax: 403-270-2772; E-mail: schryver{at}ucalgary.ca.

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

This article has been cited by other articles:

				V. Douet, D. Expert, F. Barras, and B. Py Erwinia chrysanthemi Iron Metabolism: the Unexpected Implication of the Inner Membrane Platform within the Type II Secretion System J. Bacteriol., February 1, 2009; 191(3): 795 - 804. [Abstract] [Full Text] [PDF]

				A. Badarau, S. J. Firbank, K. J. Waldron, S. Yanagisawa, N. J. Robinson, M. J. Banfield, and C. Dennison FutA2 Is a Ferric Binding Protein from Synechocystis PCC 6803 J. Biol. Chem., May 2, 2008; 283(18): 12520 - 12527. [Abstract] [Full Text] [PDF]

				M. Miethke and M. A. Marahiel Siderophore-Based Iron Acquisition and Pathogen Control Microbiol. Mol. Biol. Rev., September 1, 2007; 71(3): 413 - 451. [Abstract] [Full Text] [PDF]