1uxh: Difference between revisions
New page: left|200px<br /> <applet load="1uxh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uxh, resolution 2.10Å" /> '''LARGE IMPROVEMENT I... |
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==About this Structure== | ==About this Structure== | ||
1UXH 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 NAD and FMR 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=1UXH OCA]]. | 1UXH 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 NAD and FMR 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=1UXH OCA]]. | ||
==Reference== | ==Reference== | ||
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface., Bjork A, Dalhus B, Mantzilas D, Sirevag R, Eijsink VG, J Mol Biol. 2004 Aug 27;341(5):1215-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15321717 15321717] | Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface., Bjork A, Dalhus B, Mantzilas D, Sirevag R, Eijsink VG, J Mol Biol. 2004 Aug 27;341(5):1215-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15321717 15321717] | ||
[[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 13:13:49 2007'' | ||
Revision as of 14:09, 30 October 2007
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LARGE IMPROVEMENT IN THE THERMAL STABILITY OF A TETRAMERIC MALATE DEHYDROGENASE BY SINGLE POINT MUTATIONS AT THE DIMER-DIMER INTERFACE
OverviewOverview
The stability of tetrameric malate dehydrogenase from the green, phototrophic bacterium Chloroflexus aurantiacus (CaMDH) is at least in, part determined by electrostatic interactions at the dimer-dimer, interface. Since previous studies had indicated that the thermal stability, of CaMDH becomes lower with increasing pH, attempts were made to increase, the stability by removal of (excess) negative charge at the dimer-dimer, interface. Mutation of Glu165 to Gln or Lys yielded a dramatic increase in, thermal stability at pH 7.5 (+23.6 -- + 23.9 degrees C increase in, apparent t(m)) and a more moderate increase at pH 4.4 (+4.6 -- + 5.4, degrees C). The drastically increased stability at neutral pH was achieved, without forfeiture of catalytic performance at low temperatures. The, crystal ... [(full description)]
About this StructureAbout this Structure
1UXH is a [Single protein] structure of sequence from [Chloroflexus aurantiacus] with NAD and FMR 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
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface., Bjork A, Dalhus B, Mantzilas D, Sirevag R, Eijsink VG, J Mol Biol. 2004 Aug 27;341(5):1215-26. PMID:15321717
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