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TitleTdfH selectively binds metal-loaded tetrameric calprotectin for zinc import.
Journal, issue, pagesCommun Biol, Vol. 5, Issue 1, Page 103, Year 2022
Publish dateJan 31, 2022
AuthorsAloke K Bera / Runrun Wu / Simone Harrison / Cynthia Nau Cornelissen / Walter J Chazin / Nicholas Noinaj /
PubMed AbstractTo 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 ...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.
External linksCommun Biol / PubMed:35102276 / PubMed Central
MethodsEM (single particle)
Resolution6.05 Å
Structure data

EMDB-25692:
The 6.1 angstrom cryoEM map of calprotectin bound to TdfH
Method: EM (single particle) / Resolution: 6.05 Å

Source
  • Neisseria gonorrhoeae (bacteria)

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