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

Brian Weitzner, Thomas Meehan, Qifang Xu, Roland L. Dunbrack

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)289-295
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Volume75
Issue number2
DOIs
StatePublished - May 1 2009

Keywords

  • Animals
  • Arabidopsis Proteins/chemistry
  • Crystallography, X-Ray
  • Cytosol/enzymology
  • Databases, Protein
  • Humans
  • Hydrogen Bonding
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Sulfotransferases/chemistry

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