5UYV
YfeA ancillary sites that do not co-load with site 2
5UYV の概要
エントリーDOI | 10.2210/pdb5uyv/pdb |
関連するPDBエントリー | 5uxs |
分子名称 | Periplasmic chelated iron-binding protein YfeA, ZINC ION (3 entities in total) |
機能のキーワード | polyspecific, transition metal, transport, metal transport |
由来する生物種 | Yersinia pestis |
細胞内の位置 | Periplasm: Q56952 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 36310.44 |
構造登録者 | |
主引用文献 | Radka, C.D.,DeLucas, L.J.,Wilson, L.S.,Lawrenz, M.B.,Perry, R.D.,Aller, S.G. Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites. Acta Crystallogr D Struct Biol, 73:557-572, 2017 Cited by PubMed Abstract: Gram-negative bacteria use siderophores, outer membrane receptors, inner membrane transporters and substrate-binding proteins (SBPs) to transport transition metals through the periplasm. The SBPs share a similar protein fold that has undergone significant structural evolution to communicate with a variety of differentially regulated transporters in the cell. In Yersinia pestis, the causative agent of plague, YfeA (YPO2439, y1897), an SBP, is important for full virulence during mammalian infection. To better understand the role of YfeA in infection, crystal structures were determined under several environmental conditions with respect to transition-metal levels. Energy-dispersive X-ray spectroscopy and anomalous X-ray scattering data show that YfeA is polyspecific and can alter its substrate specificity. In minimal-media experiments, YfeA crystals grown after iron supplementation showed a threefold increase in iron fluorescence emission over the iron fluorescence emission from YfeA crystals grown from nutrient-rich conditions, and YfeA crystals grown after manganese supplementation during overexpression showed a fivefold increase in manganese fluorescence emission over the manganese fluorescence emission from YfeA crystals grown from nutrient-rich conditions. In all experiments, the YfeA crystals produced the strongest fluorescence emission from zinc and could not be manipulated otherwise. Additionally, this report documents the discovery of a novel surface metal-binding site that prefers to chelate zinc but can also bind manganese. Flexibility across YfeA crystal forms in three loops and a helix near the buried metal-binding site suggest that a structural rearrangement is required for metal loading and unloading. PubMed: 28695856DOI: 10.1107/S2059798317006349 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.691 Å) |
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