Crystal structure of the intrinsically flexible addiction antidote MazE

Remy Loris*, Irina Marianovsky, Jurij Lah, Toon Laeremans, Hanna Engelberg-Kulka, Gad Glaser, Serge Muyldermans, Lode Wyns

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

107 Scopus citations


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 β-hairpins connected by a short α-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 β-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.

Original languageAmerican English
Pages (from-to)28252-28257
Number of pages6
JournalJournal of Biological Chemistry
Issue number30
StatePublished - 25 Jul 2003


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