2CB3
Crystal structure of peptidoglycan recognition protein-LE in complex with tracheal cytotoxin (monomeric diaminopimelic acid-type peptidoglycan)
Summary for 2CB3
| Entry DOI | 10.2210/pdb2cb3/pdb |
| Descriptor | PEPTIDOGLYCAN-RECOGNITION PROTEIN-LE, GLYCEROL, GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA, ... (4 entities in total) |
| Functional Keywords | pgrp, tracheal cytotoxin, innate immunity, immune system |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Cellular location | Secreted: Q9VXN9 |
| Total number of polymer chains | 4 |
| Total formula weight | 83922.61 |
| Authors | Lim, J.-H.,Kim, M.-S.,Oh, B.-H. (deposition date: 2005-12-29, release date: 2006-01-26, Last modification date: 2023-12-13) |
| Primary citation | Lim, J.-H.,Kim, M.-S.,Kim, H.-E.,Yano, T.,Oshima, Y.,Aggarwal, K.,Goldman, W.E.,Silverman, N.,Kurata, S.,Oh, B.-H. Structural Basis for Preferential Recognition of Diaminopimelic Acid-Type Peptidoglycan by a Subset of Peptidoglycan Recognition Proteins J.Biol.Chem., 281:8286-, 2006 Cited by PubMed Abstract: Drosophila peptidoglycan recognition protein (PGRP)-LCx and -LCa are receptors that preferentially recognize meso-diaminopimelic acid (DAP)-type peptidoglycan (PGN) present in Gram-negative bacteria over lysine-type PGN of gram-positive bacteria and initiate the IMD signaling pathway, whereas PGRP-LE plays a synergistic role in this process of innate immune defense. How these receptors can distinguish the two types of PGN remains unclear. Here the structure of the PGRP domain of Drosophila PGRP-LE in complex with tracheal cytotoxin (TCT), the monomeric DAP-type PGN, reveals a buried ionic interaction between the unique carboxyl group of DAP and a previously unrecognized arginine residue. This arginine is conserved in the known DAP-type PGN-interacting PGRPs and contributes significantly to the affinity of the protein for the ligand. Unexpectedly, TCT induces infinite head-to-tail dimerization of PGRP-LE, in which the disaccharide moiety, but not the peptide stem, of TCT is positioned at the dimer interface. A sequence comparison suggests that TCT induces heterodimerization of the ectodomains of PGRP-LCx and -LCa in a closely analogous manner to prime the IMD signaling pathway, except that the heterodimer formation is nonperpetuating. PubMed: 16428381DOI: 10.1074/JBC.M513030200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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