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TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import.


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.

SUBMITTER: Bera AK 

PROVIDER: S-EPMC8803948 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature

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TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import.

Bera Aloke K AK   Wu Runrun R   Harrison Simone S   Cornelissen Cynthia Nau CN   Chazin Walter J WJ   Noinaj Nicholas N  

Communications biology 20220131 1


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. ...[more]

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