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Weitzner B , Meehan T , Xu QF , Dunbrack RL
An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases
Proteins-Structure Function and Bioinformatics. 2009 May;75(2) :289-295
PMCID: PMC 2728805   
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Abstract
Cytosolic sulfotransferases catalyze the sulforiation 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 A (FEBS Lett 2001;490:3943) 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.
Notes
Weitzner, Brian Meehan, Thomas Xu, Qifang Dunbrack, Roland L., Jr. WILEY-LISS 418SP