1ur5: Difference between revisions
New page: left|200px<br /> <applet load="1ur5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ur5, resolution 1.75Å" /> '''STABILIZATION OF A ... |
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==About this Structure== | ==About this Structure== | ||
1UR5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus]] with CD, CL, NA and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UR5 OCA]]. | 1UR5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus]] with CD, CL, NA and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UR5 OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14636605 14636605] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14636605 14636605] | ||
[[Category: Chloroflexus aurantiacus]] | [[Category: Chloroflexus aurantiacus]] | ||
[[Category: Malate dehydrogenase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bjork, A.]] | [[Category: Bjork, A.]] | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:24:03 2007'' | ||
Revision as of 14:19, 30 October 2007
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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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