2XZ4

Crystal structure of the LFZ ectodomain of the peptidoglycan recognition protein LF

Summary for 2XZ4

• Entry DOI: 10.2210/pdb2xz4/pdb
• Related: 2XZ8
• Descriptor: PEPTIDOGLYCAN-RECOGNITION PROTEIN LF, COPPER (II) ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: immune system, innate immunity
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Cellular location: Membrane; Multi-pass membrane protein (Potential): Q8SXQ7
• Total number of polymer chains: 2
• Total formula weight: 41698.82

Authors

Basbous, N.,Coste, F.,Leone, P.,Vincentelli, R.,Royet, J.,Kellenberger, C.,Roussel, A. (deposition date: 2010-11-23, release date: 2011-04-13, Last modification date: 2023-12-20)

Primary citation

Basbous, N.,Coste, F.,Leone, P.,Vincentelli, R.,Royet, J.,Kellenberger, C.,Roussel, A.
The Drosophila Peptidoglycan-Recognition Protein Lf Interacts with Peptidoglycan-Recognition Protein Lc to Downregulate the Imd Pathway.
Embo Rep., 12:327-, 2011

PubMed Abstract: The peptidoglycan (PGN)-recognition protein LF (PGRP-LF) is a specific negative regulator of the immune deficiency (Imd) pathway in Drosophila. We determine the crystal structure of the two PGRP domains constituting the ectodomain of PGRP-LF at 1.72 and 1.94 Å resolution. The structures show that the LFz and LFw domains do not have a PGN-docking groove that is found in other PGRP domains, and they cannot directly interact with PGN, as confirmed by biochemical-binding assays. By using surface plasmon resonance analysis, we show that the PGRP-LF ectodomain interacts with the PGRP-LCx ectodomain in the absence and presence of tracheal cytotoxin. Our results suggest a mechanism for downregulation of the Imd pathway on the basis of the competition between PRGP-LCa and PGRP-LF to bind to PGRP-LCx.

PubMed: 21372849
DOI: 10.1038/EMBOR.2011.19

Experimental method

X-RAY DIFFRACTION (1.72 Å)