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1z6i

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1z6i, resolution 2.50Å

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Crystal structure of the ectodomain of Drosophila transmembrane receptor PGRP-LCa

Overview

The peptidoglycan-recognition protein LCa (PGRP-LCa) is a transmembrane, receptor required for activation of the Drosophila immune deficiency, pathway by monomeric Gram-negative peptidoglycan. We have determined the, crystal structure of the ectodomain of PGRP-LCa at 2.5-A resolution and, found two unique helical insertions in the LCa ectodomain that disrupt an, otherwise L-shaped peptidoglycan-docking groove present in all other known, PGRP structures. The deficient binding of PGRP-LCa to monomeric, peptidoglycan was confirmed by biochemical pull-down assays. Recognition, of monomeric peptidoglycan involves both PGRP-LCa and -LCx. We showed that, association of the LCa and LCx ectodomains in vitro depends on monomeric, peptidoglycan. The presence of a defective peptidoglycan-docking groove, while preserving a unique role in mediating monomeric peptidoglycan, induction of immune response, suggests that PGRP-LCa recognizes the, exposed structural features of a monomeric muropeptide when the latter is, bound to and presented by the ectodomain of PGRP-LCx. Such features, include N-acetyl glucosamine and the anhydro bond in the glycan of the, muropeptide, which have been demonstrated to be critical for immune, stimulatory activity.

About this Structure

1Z6I is a Single protein structure of sequence from Drosophila melanogaster with NAG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition., Chang CI, Ihara K, Chelliah Y, Mengin-Lecreulx D, Wakatsuki S, Deisenhofer J, Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10279-84. Epub 2005 Jul 8. PMID:16006509

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