Biomolecular NMR Laboratory, I.R.C.C.S. Ospedale San Raffaele, Via Olgettina 58, 20132 Milan, Italy.
Unit of Immunogenetics, Leukemia Genomics and Immunobiology and Center for Omics Sciences, I.R.C.C.S. Ospedale San Raffaele, Via Olgettina 58, 20132 Milan, Italy.
ACS Chem Biol. 2022 Jan 21;17(1):230-239. doi: 10.1021/acschembio.1c00886. Epub 2021 Dec 30.
The SYLF domain is an evolutionary conserved protein domain with phosphatidylinositol binding ability, whose three-dimensional structure is unknown. Here, we present the solution structure and the dynamics characterization of the SYLF domain of the bacterial BPSL1445 protein. BPSL1445 is a seroreactive antigen and a diagnostic marker of , the etiological agent of melioidosis, a severe infectious disease in the tropics. The BPSL1445 SYLF domain (BPSL1445-SYLF) consists of a β-barrel core, with two flexible loops protruding out of the barrel and three helices packing on its surface. Our structure allows for a more precise definition of the boundaries of the SYLF domain compared to the previously reported one and suggests common ancestry with bacterial EipA domains. We also demonstrate by phosphatidyl-inositol phosphate arrays and nuclear magnetic resonance titrations that BPSL1445-SYLF weakly interacts with phosphoinositides, thus supporting lipid binding abilities of this domain also in prokaryotes.
SYLF 结构域是一种具有磷酸肌醇结合能力的进化保守蛋白结构域，其三维结构未知。本文介绍了细菌 BPSL1445 蛋白的 SYLF 结构域的溶液结构和动力学特征。BPSL1445 是一种血清反应性抗原，也是类鼻疽伯克霍尔德菌的诊断标志物，类鼻疽伯克霍尔德菌是热带地区一种严重的传染病病原体。BPSL1445-SYLF 结构域（BPSL1445-SYLF）由一个β-桶核心组成，有两个柔性环从桶中伸出，三个螺旋在其表面堆积。与之前报道的结构相比，我们的结构可以更精确地定义 SYLF 结构域的边界，并表明其与细菌 EipA 结构域具有共同的祖先。我们还通过磷酯酰肌醇磷酸盐阵列和核磁共振滴定证明，BPSL1445-SYLF 与磷酸肌醇弱相互作用，因此支持该结构域在原核生物中也具有脂质结合能力。
