Crystal structure of the intrinsically flexible addiction antidote MazE.

TitleCrystal structure of the intrinsically flexible addiction antidote MazE.
Publication TypeJournal Article
Year of Publication2003
AuthorsLoris, R., I. Marianovsky, J. Lah, T. Laeremans, H. Engelberg-Kulka, G. Glaser, S. Muyldermans, and L. Wyns
JournalJ Biol Chem
Volume278
Issue30
Pagination28252-7
Date Published2003 Jul 25
ISSN0021-9258
KeywordsAmino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Camels, Crystallography, X-Ray, DNA, DNA-Binding Proteins, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid
Abstract

A specific camel VHH (variable domain of dromedary heavy chain antibody) fragment was used to crystallize the intrinsically flexible addiction antidote MazE. Only 45% of the polypeptide chain is found ordered in the crystal. The MazE monomer consisting of two beta-hairpins connected by a short alpha-helix has no hydrophobic core on its own and represents only one half of a typical protein domain. A complete domain structure is formed by the association of two chains, creating a hydrophobic core between two four-stranded beta-sheets. This hydrophobic core consists exclusively of short aliphatic residues. The folded part of MazE contains a novel DNA binding motif. A model for DNA binding that is consistent with the available biochemical data is presented.

DOI10.1074/jbc.M302336200
Alternate JournalJ. Biol. Chem.
PubMed ID12743116