Structural highlights
Function
[PGPLB_DROME] N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The family of peptidoglycan recognition proteins (PGRPs) are associated with the recognition of the peptidoglycan of microbes and subsequent activation of signaling pathways for immune response. Here the crystal structure of Drosophila PGRP-LB is determined at a resolution of 2.0 A and shows an active-site cleft with a zinc cage. Poor conservation of surface residues at the cleft predicts a widely varying individual specificity of PGRPs for molecular patterns on microbial cell walls. At the back of this cleft is a putatively conserved distinctive groove. The location and mainly hydrophobic nature of the groove indicate that the back face serves for subsequent signaling after clustering of PGRP molecules by binding to polymeric cell wall components.
Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster.,Kim MS, Byun M, Oh BH Nat Immunol. 2003 Aug;4(8):787-93. Epub 2003 Jul 6. PMID:12845326[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim MS, Byun M, Oh BH. Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat Immunol. 2003 Aug;4(8):787-93. Epub 2003 Jul 6. PMID:12845326 doi:10.1038/ni952
- ↑ Kim MS, Byun M, Oh BH. Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat Immunol. 2003 Aug;4(8):787-93. Epub 2003 Jul 6. PMID:12845326 doi:10.1038/ni952
