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Papers In Press, published online ahead of print May 12, 2004
Center for Advanced Research in Biotechnology, University of Maryland, Rockville, MD 20850
Corresponding Author: mariuzza{at}carb.nist.gov
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate immune system that bind, and in some cases hydrolyze, peptidoglycans (PGNs) on bacterial cell walls. These molecules, which are highly conserved from insects to mam mals, participate in host defense against both Gram-positive and Gram-negative bacteria. We report the crystal structure of the C-terminal PGN-binding domain of human PGRP-I
J. Biol. Chem, 10.1074/jbc.M404920200
Submitted on May 3, 2004
Revised on May 12, 2004
Accepted on May 12, 2004
Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein I
in two oligomeric states, monomer and dimer, to resolutions of 2.80 * n and 1.65 * n, respectively. In contrast to PGRPs with PGN-lytic amidase activity, no zinc ion is present in the PGN-binding site of human PGRP-I. The structure reveals that PGRPs exhibit extensive topological variability in a large hydrophobic groove, located opposite the PGN-binding site, which may recognize host effector proteins or microbial ligands other than PGN. We also show that full-length PGRP-I comprises two tandem PGN-binding domains. These domains differ at most potential PGN-contacting positions, implying different fine specificities. Dimerization of PGRP-I, which occurs through three-dimensional domain swapping, is mediated by specific binding of sodium ions to a flexible hinge loop, stabilizing the conformation found in the dimer. We further demonstrate sodium-dependent dimerization of PGRP-I in solution, suggesting a possible mechanism for modulating PGRP activity through the formation of multivalent adducts.
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