1MVF

MazE addiction antidote

Summary for 1MVF

• Entry DOI: 10.2210/pdb1mvf/pdb
• Descriptor: immunoglobulin heavy chain variable region, PemI-like protein 1 (3 entities in total)
• Functional Keywords: plasmid addiction, camel antibody, addiction antidote, immune system
• Biological source: Camelus dromedarius (Arabian camel); More
• Total number of polymer chains: 4
• Total formula weight: 48516.33

Authors

Loris, R.,Marianovsky, I.,Lah, J.,Laeremans, T.,Engelberg-Kulka, H.,Glaser, G.,Muyldermans, S.,Wyns, L. (deposition date: 2002-09-25, release date: 2003-06-10, Last modification date: 2024-10-30)

Primary citation

Loris, R.,Marianovsky, I.,Lah, J.,Laeremans, T.,Engelberg-Kulka, H.,Glaser, G.,Muyldermans, S.,Wyns, L.
Crystal structure of the intrinsically flexible addiction antidote MazE.
J.Biol.Chem., 278:28252-28257, 2003

PubMed 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.

PubMed: 12743116
DOI: 10.1074/jbc.M302336200

Experimental method

X-RAY DIFFRACTION (1.65 Å)