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J. Biol. Chem., Vol. 280, Issue 19, 19045-19050, May 13, 2005

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1.6-Å Crystal Structure of EntA-im

A BACTERIAL IMMUNITY PROTEIN CONFERRING IMMUNITY TO THE ANTIMICROBIAL ACTIVITY OF THE PEDIOCIN-LIKE BACTERIOCIN ENTEROCIN A^*

Line Johnsen¶, Bjørn Dalhus||, Ingar Leiros**, and Jon Nissen-Meyer

From the Program for Biochemistry and Molecular Biology, Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway, ^||Institute of Medical Microbiology, Section for Molecular Microbiology, National University Hospital, N-0027 Oslo, Norway, and ^**Macromolecular Crystallography Group, European Synchrotron Radiation Facility, BP220, F-38043 Grenoble Cedex 9, France

Many Gram-positive bacteria produce ribosomally synthesized antimicrobial peptides, often termed bacteriocins. Genes encoding pediocin-like bacteriocins are generally cotranscribed with or in close vicinity to a gene encoding a cognate immunity protein that protects the bacteriocin-producer from their own bacteriocin. We present the first crystal structure of a pediocin-like immunity protein, EntA-im, conferring immunity to the bacteriocin enterocin A. Determination of the structure of this 103-amino acid protein revealed that it folds into an antiparallel four-helix bundle with a flexible C-terminal part. The fact that the immunity protein conferring immunity to carnobacteriocin B2 also consists of a four-helix bundle (Sprules, T., Kawulka, K. E., and Vederas, J. C. (2004) Biochemistry 43, 11740–11749) strongly indicates that this is a conserved structural motif in all pediocin-like immunity proteins. The C-terminal half of the immunity protein contains a region that recognizes the C-terminal half of the cognate bacteriocin, and the flexibility in the C-terminal end of the immunity protein might thus be an important characteristic that enables the immunity protein to interact with its cognate bacteriocin. By homology modeling of three other pediocin-like immunity proteins and calculation of the surface charge distribution for EntA-im and the three structure models, different charge distributions were observed. The differences in the latter part of helix 3, the beginning of helix 4, and the loop connecting these helices might also be of importance in determining the specificity.

Received for publication, February 7, 2005 , and in revised form, March 4, 2005.

^* This work was supported by Norwegian Research Council Projects 138404/432 (to L. J.) and 138493/410 (to B. D.). The Norwegian Research Council also contributed travel expenses for the trip to European Synchrotron Radiation Facility (Grenoble, France) through the SYGOR Project. Beamline ID29 at the European Synchrotron Radiation Facility (Experiment MX159) and the Swiss-Norwegian Beamline (Experiment 01-02-633) also contributed travel expenses for project MX-159. 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.

The atomic coordinates and structure factors (codes 2BL8 and 2BL7) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Both authors contributed equally to this work.

^¶ To whom correspondence should be addressed: Dept. of Molecular Biosciences, University of Oslo, P. O. Box 1041, Blindern, 0316 Oslo, Norway. Tel.: 47-22-85-73-51; Fax: 47-22-85-44-43; E-mail: line.johnsen{at}biokjemi.uio.no.

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