title: The structural basis of transferrin sequestration by transferrin-binding protein B.
abstract: Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin.
authors.affiliation: Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Charles
authors.initials: C
authors.lastname: Calmettes
authors.forename: Joenel
authors.initials: J
authors.lastname: Alcantara
authors.forename: Rong-Hua
authors.initials: RH
authors.lastname: Yu
authors.forename: Anthony B
authors.initials: AB
authors.lastname: Schryvers
authors.forename: Trevor F
authors.initials: TF
authors.lastname: Moraes
mesh_terms: D006801:Humans; D008958:Models, Molecular; D009345:Neisseria meningitidis / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D014168:Transferrin / Q000737:chemistry* / Q000378:metabolism; D033882:Transferrin-Binding Protein B / Q000737:chemistry* / Q000378:metabolism
chemical_list: D014168:Transferrin; D033882:Transferrin-Binding Protein B