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首页> 外文期刊>Protein Science: A Publication of the Protein Society >Crystal structures of three representatives of a new Pfam family PF14869 (DUF4488) suggest they function in sugar binding/uptake
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Crystal structures of three representatives of a new Pfam family PF14869 (DUF4488) suggest they function in sugar binding/uptake

机译:新的Pfam家族PF14869(DUF4488)的三个代表的晶体结构表明它们在糖结合/摄取中起作用

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摘要

Crystal structures of three members (BACOVA_00364 from Bacteroides ovatus, BACUNI_03039 from Bacteroides uniformis and BACEGG_00036 from Bacteroides eggerthii) of the Pfam domain of unknown function (DUF4488) were determined to 1.95, 1.66, and 1.81 angstrom resolutions, respectively. The protein structures adopt an eight-stranded, calycin-like, beta-barrel fold and bind an endogenous unknown ligand at one end of the beta-barrel. The amino acids interacting with the ligand are not conserved in any other protein of known structure with this particular fold. The size and chemical environment of the bound ligand suggest binding or transport of a small polar molecule(s) as a potential function for these proteins. These are the first structural representatives of a newly defined PF14869 (DUF4488) Pfam family.
机译:确定了功能未知的Pfam域(DUF4488)的三个成员的晶体结构(卵形拟杆菌的BACOVA_00364,卵形拟杆菌的BACUNI_03039和卵形拟杆菌的BACEGG_00036)的晶体结构分别为1.95、1.66和1.81埃分辨率。蛋白质结构采用八链,类似花萼素的β-桶折叠,并在β-桶的一端结合内源性未知配体。与配体相互作用的氨基酸在具有该特定折叠的任何其他已知结构的蛋白质中均不保守。结合的配体的大小和化学环境表明小极性分子的结合或转运是这些蛋白质的潜在功能。这些是新定义的PF14869(DUF4488)Pfam系列的第一个结构代表。

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