3wi5 | pdb_00003wi5

Crystal structure of the Loop 7 mutant PorB from Neisseria meningitidis serogroup B

spinqualitylabelsall models 3wi5, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wi5 is a 1 chain structure with sequence from "diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FLC Related: 3wi4 Gene: porB, NMB2039 ("Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [OMPB1_NEIMB] Serves as a slightly cation selective porin. Publication Abstract from PubMed Among all Neisseriae species, Neisseria meningitidis and Neisseria gonorrhoeae are the only human pathogens, causative agents of bacterial meningitis and gonorrhoea, respectively. PorB, a pan-Neisseriae trimeric porin that mediates diffusive transport of essential molecules across the bacterial outer membrane, is also known to activate host innate immunity via Toll-like receptor 2 (TLR2)-mediated signaling. The molecular mechanism of PorB binding to TLR2 is not known, but it has been hypothesized that electrostatic interactions contribute to ligand/receptor binding. Strain-specific sequence variability in the surface-exposed loops of PorB which are potentially implicated in TLR2 binding, may explain the difference in TLR2-mediated cell activation in vitro by PorB homologs from the commensal Neisseriae lactamica and the pathogen N. meningitidis. Here, we report a comparative structural analysis of PorB from N. meningitidis serogroup B strain 8765 (63% sequence homology with PorB from N. meningitidis serogroup W135) and a mutant in which amino acid substitutions in the extracellular loop 7 lead to significantly reduced TLR2-dependent activity in vitro. We observe that this mutation both alters the loop conformation and causes dramatic changes of electrostatic surface charge, both of which may affect TLR2 recognition and signaling. Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition.,Kattner C, Toussi DN, Zaucha J, Wetzler LM, Ruppel N, Zachariae U, Massari P, Tanabe M J Struct Biol. 2014 Mar;185(3):440-7. doi: 10.1016/j.jsb.2013.12.006. Epub 2013, Dec 19. PMID:24361688 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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