The PA14 domain, a conserved all-β domain in bacterial toxins, enzymes, adhesins and signaling molecules
The PA14 domain, a conserved all-β domain in bacterial toxins, enzymes, adhesins and signaling molecules
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DOI：
10.1016/j.tibs.2004.05.002
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发表时间：
2004-07-01
影响因子：
13.8
通讯作者：
Galperin, MY
中科院分区：
文献类型：
--
作者：
Rigden, DJ;Mello, LV;Galperin, MY
从细菌β-葡萄糖苷酶的结构域插入序列开始的迭代数据库搜索显示，存在一个由多种细菌和真核蛋白质共享的保守结构域。这些包括其他糖苷酶、糖基转移酶、蛋白酶、酰胺酶、粘附素和细菌毒素，如炭疽保护性抗原(PA)。该结构域也存在于哺乳动物蛋白纤维囊藻蛋白中，该蛋白的突变会导致常染色体隐性遗传性多囊肾和肝病。PA的晶体结构表明，该结构域(因其在PA(20)前体肽中的位置而被命名为PA14)具有β-桶结构。PA14序列比对表明了结合功能，而不是催化作用，而PA14结构域的分布与碳水化合物结合是兼容的。
yIterative database searches starting from a domain insert sequence in bacterial beta-glucosidases reveals the presence of a conserved domain shared by a wide variety of bacterial and eukaryotic proteins. These include other glycosidases, glycosyltransferases, proteases, amidases, adhesins, and bacterial toxins such as anthrax protective antigen (PA). The domain also occurs in the mammalian protein fibrocystin, mutation of which leads to autosomal-recessive polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA(20) pro-peptide) has a beta-barrel architecture. A PA14 sequence alignment suggests a binding function, rather than a catalytic role, whereas the PA14 domain distribution is compatible with carbohydrate binding.