4xsq | pdb_00004xsq

Structure of a variable lymphocyte receptor-like protein Bf66946 from Branchiostoma floridae

spinqualitylabelsall models 4xsq, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xsq is a 2 chain structure with sequence from Branchiostoma floridae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, GOL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LRRCB_BRAFL Binds selectively to the Gram-positive bacteria S.aureus and S.pneumoniae. Does not adhere to the Gram-negative bacteria E.coli and S.enterica. Probably recognizes peptidoglycans expressed on the bacterial cell surface. Publication Abstract from PubMed Discovery of variable lymphocyte receptors (VLRs) in agnathans (jawless fish) has brought the origin of adaptive immunity system (AIS) forward to 500 million years ago accompanying with the emergence of vertebrates. Previous findings indicated that amphioxus, a representative model organism of chordate, also possesses some homologs of the basic components of TCR/BCR-based AIS, but it remains unknown if there exist any components of VLR-based AIS in amphioxus. Bioinformatics analyses revealed the amphioxus Branchiostoma floridae encodes a group of putative VLR-like proteins. Here we reported the 1.79 A crystal structure of Bf66946, which forms a crescent-shaped structure of five leucine-rich repeats (LRRs). Structural comparisons indicated that Bf66946 resembles the lamprey VLRC. Further electrostatic potential analyses showed a negatively-charged patch at the concave of LRR solenoid structure that might be responsible for antigen recognition. Site-directed mutagenesis combined with bacterial binding assays revealed that Bf66946 binds to the surface of Gram-positive bacteria Staphylococcus aureus and Streptococcus pneumonia via a couple of acidic residues at the concave. In addition, the closest homolog of Bf66946 is highly expressed in the potential immune organ gill of Branchiostoma belcheri. Altogether, our findings provide the first structural evidence for the emergence of VLR-like molecules in the basal chordates. Structure of a variable lymphocyte receptor-like protein from the amphioxus Branchiostoma floridae.,Cao DD, Liao X, Cheng W, Jiang YL, Wang WJ, Li Q, Chen JY, Chen Y, Zhou CZ Sci Rep. 2016 Jan 29;6:19951. doi: 10.1038/srep19951. PMID:26821753 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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