1mvf
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(New page: 200px<br /> <applet load="1mvf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mvf, resolution 1.65Å" /> '''MazE addiction anti...)
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Revision as of 07:30, 18 November 2007
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MazE addiction antidote
Overview
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.
About this Structure
1MVF is a Single protein structure of sequence from Camelus dromedarius and Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the intrinsically flexible addiction antidote MazE., Loris R, Marianovsky I, Lah J, Laeremans T, Engelberg-Kulka H, Glaser G, Muyldermans S, Wyns L, J Biol Chem. 2003 Jul 25;278(30):28252-7. Epub 2003 May 12. PMID:12743116
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