The structural basis of transferrin sequestration by transferrin-binding protein B

Nat Struct Mol Biol. 2012 Feb 19;19(3):358-60. doi: 10.1038/nsmb.2251.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Models, Molecular
  • Neisseria meningitidis / chemistry*
  • Neisseria meningitidis / metabolism
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Quaternary
  • Transferrin / chemistry*
  • Transferrin / metabolism
  • Transferrin-Binding Protein B / chemistry*
  • Transferrin-Binding Protein B / metabolism

Substances

  • Transferrin
  • Transferrin-Binding Protein B

Associated data

  • PDB/3VE1
  • PDB/3VE2