Title | Crystal structure of the intrinsically flexible addiction antidote MazE. |
Publication Type | Journal Article |
Year of Publication | 2003 |
Authors | Loris, R., I. Marianovsky, J. Lah, T. Laeremans, H. Engelberg-Kulka, G. Glaser, S. Muyldermans, and L. Wyns |
Journal | J Biol Chem |
Volume | 278 |
Issue | 30 |
Pagination | 28252-7 |
Date Published | 2003 Jul 25 |
ISSN | 0021-9258 |
Keywords | Amino 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. |
DOI | 10.1074/jbc.M302336200 |
Alternate Journal | J. Biol. Chem. |
PubMed ID | 12743116 |
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