Crystal structure of human catecholamine sulfotransferase
Crystal structure of human catecholamine sulfotransferase
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DOI：
10.1006/jmbi.1999.3153
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发表时间：
1999-10-29
影响因子：
5.6
通讯作者：
Martin, JL
中科院分区：
文献类型：
--
作者：
Bidwell, LM;McManus, ME;Martin, JL
与磷酸化作用一样，磺化作用可以改变多种生物分子的活性。磺基转移酶使神经递质、药物、类固醇激素、膳食致癌物和蛋白质磺化。SULT 1A 3特异性地磺化儿茶酚胺，如多巴胺、肾上腺素和去甲肾上腺素。已在2.4埃分辨率下测定了在活性位点结合有硫酸根的SULT 1A 3的晶体结构。虽然核心α/β折叠类似于雌激素和乙酰肝素磺基转移酶，但主要差异发生在活性位点及其周围。最值得注意的是，围绕活性位点的几个区域，包括40个残基的部分，在SULT 1A 3中是无序的。与SULT 1A 3的无序部分拓扑等价的区域参与雌激素和乙酰肝素磺基转移酶中的底物和辅因子结合。在这些地区的灵活性表明，配体结合eleclants和周围的磺基转移酶的活性位点的无序有序过渡，并可能有助于这些酶的广泛的底物特异性。(C)北京：科学出版社.
Sulfonation, like phosphorylation, can modify the activity of a variety of biological molecules. The sulfotransferase enzymes sulfonate neurotransmitters, drugs, steroid hormones, dietary carcinogens and proteins. SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 Angstrom resolution. Although the core alpha/beta fold is like that of estrogen and heparan sulfotransferases, major differences occur in and around the active site. Most notably, several regions Surrounding the active site, including a section of 40 residues, are disordered in SULT1A3. Regions that are topologically equivalent to the disordered parts of SULT1A3 are involved in substrate and cofactor binding in estrogen and heparan sulfotransferase. Flexibility in these regions suggests that ligand binding elicits a disorder-order transition in and around the active site of sulfotransferases and might contribute to the broad substrate specificity of these enzymes. (C) 1999 Academic Press.