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.
© 2022. The Author(s).
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Bacterial Outer Membrane Proteins / metabolism*
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Biological Transport
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Cryoelectron Microscopy
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Gene Expression Regulation, Bacterial
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Leukocyte L1 Antigen Complex / chemistry*
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Models, Molecular
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Neisseria gonorrhoeae / metabolism*
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Protein Conformation
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Zinc / metabolism*
Substances
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Bacterial Outer Membrane Proteins
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Leukocyte L1 Antigen Complex
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TdfH protein, Neisseria
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Zinc