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J. Biol. Chem., Vol. 282, Issue 27, 19629-19637, July 6, 2007

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The Enterococcus faecalis MSCRAMM ACE Binds Its Ligand by the Collagen Hug Model^*

Qing Liu¹, Karthe Ponnuraj¹, Yi Xu, Vannakambadi K. Ganesh, Jouko Sillanpää^¶, Barbara E. Murray^¶, Sthanam V. L. Narayana^||, and Magnus Höök²

From the Center for Extracellular Matrix Biology, Texas A&M University System Health Science Center, Albert B. Alkek Institute of Biosciences and Technology, Houston, Texas 77030, the ^||School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama 35294, the ^¶Division of Infectious Diseases, Department of Internal Medicine, and Center for the Study of Emerging and Re-emerging Pathogens, University of Texas Medical School at Houston, Houston, Texas 77030, and the Department of Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600025, India

We have determined the crystal structure of the ligand binding segment of the Enterococcus faecalis collagen binding MSCRAMM ACE (microbial surface components recognizing adhesive matrix molecules adhesin of collagen from enterococci). This segment is composed of two subdomains, N₁ and N₂, each adopting an IgG-like fold and forming a putative collagen binding surface at the interface between the two subdomains. This structure is very similar to that recently reported for CNA, the collagen binding MSCRAMM of Staphylococcus aureus, for which a unique ligand binding mechanism called the Collagen Hug was proposed. We suggest that ACE binds collagen by a similar mechanism and present the first biochemical evidence for this binding model. Replacing residues in the putative collagen binding trench of ACE N₂ with Ala residues affected collagen binding. A closed conformation of ACE stabilized by an engineered disulfide bond is unable to bind collagen. Finally, the importance of the residues in the N₂ extension in stabilizing the MSCRAMM-ligand complex is demonstrated by selected point and truncation mutations.

Received for publication, December 5, 2006 , and in revised form, March 23, 2007.

The atomic coordinates and structure factors (code 2Z1P) 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 National Institutes of Health Grants AI 20624 (to M. H.) and R37 AI 47923 (to B. E. M.). 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 on-line version of this article (available at http://www.jbc.org) contains a supplemental table.

¹ Both authors contributed equally to this work.

² To whom correspondence should be addressed: Center for Extracellular Matrix Biology, TX A&M University System Health Science Center, Institute of Biosciences and Technology, 2121 West Holcombe Blvd., Suite 603, Houston, TX 77030, Tel.: 713-677-7552; Fax: 713-677-7576; E-mail: mhook{at}ibt.tamhsc.edu.

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