An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases.
An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases.
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DOI：
10.1002/prot.22347
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发表时间：
2009-05-01
影响因子：
2.9
通讯作者：
Dunbrack, Roland L., Jr.
中科院分区：
文献类型：
--
作者：
Weitzner, Brian;Meehan, Thomas;Xu, Qifang;Dunbrack, Roland L., Jr.
Cytosolic sulfotransferases catalyze the sulfonation of hormones, metabolites, and xenobiotics. Many of these proteins have been shown to form homo- and heterodimers. An unusually small dimer interface was previously identified by Petrotchenko et al. (FEBS Lett 490, 39-43, 2001) by crosslinking, protease digestion, and mass spectrometry, and verified by site-directed mutagenesis. Analysis of the crystal packing interfaces in all 28 available crystal structures consisting of 17 crystal forms shows that this interface occurs in all of them. With a small number of exceptions, the publicly available databases of biological assemblies contain either monomers or incorrect dimers. Even crystal structures of mouse SULT1E1, which is a monomer in solution, contain the common dimeric interface, although distorted and missing two important salt bridges.
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