1ur5: Difference between revisions
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STABILIZATION OF A TETRAMERIC MALATE DEHYDROGENASE BY INTRODUCTION OF A DISULFIDE BRIDGE AT THE DIMER/DIMER INTERFACE
OverviewOverview
Malate dehydrogenase (MDH) from the moderately thermophilic bacterium, Chloroflexus aurantiacus (CaMDH) is a tetrameric enzyme, while MDHs from, mesophilic organisms usually are dimers. To investigate the potential, contribution of the extra dimer-dimer interface in CaMDH with respect to, thermal stability, we have engineered an intersubunit disulfide bridge, designed to strengthen dimer-dimer interactions. The resulting mutant, (T187C, containing two 187-187 disulfide bridges in the tetramer) showed a, 200-fold increase in half-life at 75 degrees C and an increase of 15 deg., C in apparent melting temperature compared to the wild-type. The crystal, structure of the mutant (solved at 1.75 A resolution) was essentially, identical with that of the wild-type, with the exception of the added, ... [(full description)]
About this StructureAbout this Structure
1UR5 is a [Single protein] structure of sequence from [Chloroflexus aurantiacus] with CD, CL, NA and NAD as [ligands]. Active as [Malate dehydrogenase], with EC number [1.1.1.37]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interface., Bjork A, Dalhus B, Mantzilas D, Eijsink VG, Sirevag R, J Mol Biol. 2003 Dec 5;334(4):811-21. PMID:14636605
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