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An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases
Author(s) -
Weitzner Brian,
Meehan Thomas,
Xu Qifang,
Dunbrack Roland L.
Publication year - 2009
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22347
Subject(s) - dimer , monomer , chemistry , crystal (programming language) , crystallography , mutagenesis , crystal structure , stereochemistry , biochemistry , polymer , organic chemistry , mutation , gene , computer science , programming language
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. Proteins 2009. © 2008 Wiley‐Liss, Inc.