2F2L

Crystal structure of tracheal cytotoxin (TCT) bound to the ectodomain complex of peptidoglycan recognition proteins LCa (PGRP-LCa) and LCx (PGRP-LCx)

Summary for 2F2L

• Entry DOI: 10.2210/pdb2f2l/pdb
• Descriptor: Peptidoglycan-recognition protein-LC isoform LCa, Peptidoglycan recognition protein-LC isoform LCx, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: protein-peptidoglycan complex, membrane protein, immune system, toxin
• Biological source: Drosophila melanogaster (fruit fly); More
• Total number of polymer chains: 2
• Total formula weight: 39538.57

Authors

Chang, C.I.,Deisenhofer, J. (deposition date: 2005-11-17, release date: 2006-04-04, Last modification date: 2024-11-20)

Primary citation

Chang, C.I.,Chelliah, Y.,Borek, D.,Mengin-Lecreulx, D.,Deisenhofer, J.
Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor.
Science, 311:1761-1764, 2006

PubMed Abstract: Tracheal cytotoxin (TCT), a naturally occurring fragment of Gram-negative peptidoglycan, is a potent elicitor of innate immune responses in Drosophila. It induces the heterodimerization of its recognition receptors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficiency pathway. The crystal structure at 2.1 angstrom resolution of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the LCx ectodomain for recognition by the LCa ectodomain; the latter lacks a canonical peptidoglycan-docking groove conserved in other PGRPs. The interface, revealed in atomic detail, between TCT and the receptor complex highlights the importance of the anhydro-containing disaccharide in bridging the two ectodomains together and the critical role of diaminopimelic acid as the specificity determinant for PGRP interaction.

PubMed: 16556841
DOI: 10.1126/science.1123056

Experimental method

X-RAY DIFFRACTION (2.1 Å)