TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import

Commun Biol. 2022 Jan 31;5(1):103. doi: 10.1038/s42003-022-03039-y.

Abstract

To combat nutritional immunity, N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP). Here, we report the 6.1 Å cryoEM structure of the gonococcal surface receptor TdfH in complex with a zinc-bound CP tetramer. We further show that TdfH can also interact with CP in the presence of copper and manganese, but not with cobalt.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacterial Outer Membrane Proteins / metabolism*
  • Biological Transport
  • Cryoelectron Microscopy
  • Gene Expression Regulation, Bacterial
  • Leukocyte L1 Antigen Complex / chemistry*
  • Models, Molecular
  • Neisseria gonorrhoeae / metabolism*
  • Protein Conformation
  • Zinc / metabolism*

Substances

  • Bacterial Outer Membrane Proteins
  • Leukocyte L1 Antigen Complex
  • TdfH protein, Neisseria
  • Zinc