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-Structure paper
| タイトル | Structural insights into zinc piracy by Neisseria gonorrhoeae to overcome nutritional immunity. |
|---|---|
| ジャーナル・号・ページ | Structure, Vol. 34, Issue 2, Page 322-333.e6, Year 2026 |
| 掲載日 | 2026年2月5日 |
著者 | Pooneh Tavakoley Gheinani / Aloke Bera / Julie Stoudenmire-Saylor / Yi Lien / Simone A Harrison / Alison Criss / Walter J Chazin / Nicholas Noinaj / Cynthia Nau Cornelissen / ![]() |
| PubMed 要旨 | With an estimated 106 million global cases annually, Neisseria gonorrhoeae (Ngo) poses a significant public health problem. Ngo demonstrates a remarkable capacity to overcome nutritional immunity ...With an estimated 106 million global cases annually, Neisseria gonorrhoeae (Ngo) poses a significant public health problem. Ngo demonstrates a remarkable capacity to overcome nutritional immunity through the deployment of specialized transporters that pirate metals such as zinc from human proteins such as calprotectin (hCP). We report the cryo-EM structure of Ngo TdfH in complex with a heterotetramer of hCP. An extensive binding interface is mediated almost entirely by the S100A9 subunits of hCP. Mutagenesis studies of residues in the large binding interface reveal minimal effects from single-site mutations, whereas larger truncations disrupt binding and function. These results support a mechanistic model based on the large interaction interface overcoming a steric clash between α-helix III of S100A9 and loops 5 and 9 of TdfH, which leads to the distortion of the proximal His6 site, followed by zinc release, and import through the barrel domain. |
リンク | Structure / PubMed:41418777 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.67 Å |
| 構造データ | EMDB-70277, PDB-9oaa: |
| 化合物 | ![]() ChemComp-CA: ![]() ChemComp-ZN: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / outer membrane protein / metal transport / gram-negative bacteria / Neisseria / tonB dependent transporter |
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neisseria gonorrhoeae fa 1090 (淋菌)
homo sapiens (ヒト)
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