An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases

PROTEINS: Structure, Function, and Bioinformatics, 2009: https://doi.org/10.1002/prot.22347

Suggested citation: Weitzner B, Meehan T, Xu Q, Dunbrack R (2009) “An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases,” Proteins. 75(2), 1097–134. DOI:0.1002/prot.22347

Abstract: Cytosolic sulfotransferases catalyze the sulfonation of hormones, metabolites, and xenobiotics. Many of these proteins have been shown to form homodimers and heterodimers. An unusually small dimer interface was previously identified by Petrotchenko et al. (FEBS Lett 2001;490:39–43) by cross‐linking, 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.