TY - JOUR
T1 - An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases
AU - Weitzner, Brian
AU - Meehan, Thomas
AU - Xu, Qifang
AU - Dunbrack, Roland L.
PY - 2009/5/1
Y1 - 2009/5/1
N2 - Cytosolic sulfotransferases catalyze the sulfonation of hormones, metabolites, and xeno-biotics. Many of these proteins have been shown to form homodimers and hetero-dimers. 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 spectrome-try and verified by site-directed mutagenesis. Analysis of the crystal packing interfaces in all 28 available crystal structures consisting of 17 crystal forms showsthatthisinterfaceoccurs 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.
AB - Cytosolic sulfotransferases catalyze the sulfonation of hormones, metabolites, and xeno-biotics. Many of these proteins have been shown to form homodimers and hetero-dimers. 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 spectrome-try and verified by site-directed mutagenesis. Analysis of the crystal packing interfaces in all 28 available crystal structures consisting of 17 crystal forms showsthatthisinterfaceoccurs 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.
KW - Animals
KW - Arabidopsis Proteins/chemistry
KW - Crystallography, X-Ray
KW - Cytosol/enzymology
KW - Databases, Protein
KW - Humans
KW - Hydrogen Bonding
KW - Protein Conformation
KW - Protein Interaction Domains and Motifs
KW - Protein Multimerization
KW - Sulfotransferases/chemistry
UR - http://www.scopus.com/inward/record.url?scp=66149131846&partnerID=8YFLogxK
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=purepublist2023&SrcAuth=WosAPI&KeyUT=WOS:000264169400003&DestLinkType=FullRecord&DestApp=WOS
U2 - 10.1002/prot.22347
DO - 10.1002/prot.22347
M3 - Article
C2 - 19173308
SN - 0887-3585
VL - 75
SP - 289
EP - 295
JO - Proteins: Structure, Function and Bioinformatics
JF - Proteins: Structure, Function and Bioinformatics
IS - 2
ER -