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

TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import.
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TdfH选择性结合负载金属的四聚体钙卫蛋白用于锌输入。

DOI:
10.1038/s42003-022-03039-y
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发表时间:
2022-01-31
影响因子:
5.9
通讯作者:
Noinaj N
Noinaj N
中科院分区:
生物学2区
文献类型:
--
作者:
Bera AK;Wu R;Harrison S;Cornelissen CN;Chazin WJ;Noinaj N

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为了对抗营养免疫,N.淋病已经进化出直接从宿主金属结合蛋白如钙卫蛋白(CP)劫持锌和其它金属的系统。在这里,我们报告的6.1 μ m cryoEM结构的淋球菌表面受体TdfH在复杂的锌结合CP四聚体。我们进一步表明,TdfH也可以在铜和锰的存在下与CP相互作用,但不与钴。人类对病原体的防御机制涉及限制必需营养素,例如锌,其被从人类钙卫蛋白中掠夺锌的表面受体TdfH抵消。TdfH cryo-EM结构来自N.淋病与钙卫蛋白四聚体的复合物提供了对蛋白质-蛋白质相互作用和金属离子作用的深入了解。
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. The human defense mechanism against pathogens involves limiting essential nutrients, such as zinc which is countered by surface receptor TdfH pirating zinc from human calprotectin. The TdfH cryo-EM structure from N. gonorrhoeae in complex with a calprotectin tetramer provides insights into the protein-protein interaction and the role of metal ions.
DOI: 10.1371/journal.ppat.1003733
发表时间: 2013-10
期刊: PLoS pathogens
影响因子: 6.7
作者:
Stork M;Grijpstra J;Bos MP;Mañas Torres C;Devos N;Poolman JT;Chazin WJ;Tommassen J
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