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Crystal structure of the intrinsically flexible addiction antidote MazE

Publication Type:

Journal Article

Authors:

Loris,R.; Marianovsky,I.; Lah,J.; Laeremans,T.; Engelberg-Kulka,H.; Glaser,G.; Muyldermans,S.; Wyns,L.

Source:

Volume 278, Issue 30, p.28252 - 28257 (2003)

URL:

PM:12743116

Keywords:

Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites; Camels; Crystallography; X-Ray; Dna; metabolism; DNA-Binding Proteins; chemistry; physiology; Escherichia coli; Escherichia coli Proteins; Models; Molecular; Molecular Sequence Data; Mutation;

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

Notes:

DA - 20030721
IS - 0021-9258 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (DNA-Binding Proteins)
RN - 0 (Escherichia coli Proteins)
RN - 0 (MazE protein, E coli)
RN - 9007-49-2 (DNA)
SB - IM