6Y4E
X-ray structure of the Zn-dependent receptor-binding domain of Proteus mirabilis MR/P fimbrial adhesin MrpH
6Y4E の概要
| エントリーDOI | 10.2210/pdb6y4e/pdb |
| 分子名称 | Fimbrial adhesin, ZINC ION, L(+)-TARTARIC ACID, ... (4 entities in total) |
| 機能のキーワード | metal binding protein, fimbrial adhesin, cell adhesion |
| 由来する生物種 | Proteus mirabilis (strain HI4320) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15262.30 |
| 構造登録者 | |
| 主引用文献 | Jiang, W.,Ubhayasekera, W.,Breed, M.C.,Norsworthy, A.N.,Serr, N.,Mobley, H.L.T.,Pearson, M.M.,Knight, S.D. MrpH, a new class of metal-binding adhesin, requires zinc to mediate biofilm formation. Plos Pathog., 16:e1008707-e1008707, 2020 Cited by PubMed Abstract: Proteus mirabilis, a Gram-negative uropathogen, is a major causative agent in catheter-associated urinary tract infections (CAUTI). Mannose-resistant Proteus-like fimbriae (MR/P) are crucially important for P. mirabilis infectivity and are required for biofilm formation and auto-aggregation, as well as for bladder and kidney colonization. Here, the X-ray crystal structure of the MR/P tip adhesin, MrpH, is reported. The structure has a fold not previously described and contains a transition metal center with Zn2+ coordinated by three conserved histidine residues and a ligand. Using biofilm assays, chelation, metal complementation, and site-directed mutagenesis of the three histidines, we show that an intact metal binding site occupied by zinc is essential for MR/P fimbria-mediated biofilm formation, and furthermore, that P. mirabilis biofilm formation is reversible in a zinc-dependent manner. Zinc is also required for MR/P-dependent agglutination of erythrocytes, and mutation of the metal binding site renders P. mirabilis unfit in a mouse model of UTI. The studies presented here provide important clues as to the mechanism of MR/P-mediated biofilm formation and serve as a starting point for identifying the physiological MR/P fimbrial receptor. PubMed: 32780778DOI: 10.1371/journal.ppat.1008707 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.02 Å) |
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