4cmf: Difference between revisions
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==The (R)-selective transaminase from Nectria haematococca with inhibitor bound== | ==The (R)-selective transaminase from Nectria haematococca with inhibitor bound== | ||
<StructureSection load='4cmf' size='340' side='right' caption='[[4cmf]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='4cmf' size='340' side='right'caption='[[4cmf]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cmf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4cmf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nectria_haematococca_mpvi Nectria haematococca mpvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CMF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PXG:3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC+ACID'>PXG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PXG:3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC+ACID'>PXG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmd|4cmd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmd|4cmd]]</td></tr> | ||
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==See Also== | ==See Also== | ||
*[[Aminotransferase|Aminotransferase]] | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Branched-chain-amino-acid transaminase]] | [[Category: Branched-chain-amino-acid transaminase]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Nectria haematococca mpvi]] | |||
[[Category: Hailes, H C]] | [[Category: Hailes, H C]] | ||
[[Category: Isupov, M]] | [[Category: Isupov, M]] | ||
Revision as of 12:25, 20 March 2019
The (R)-selective transaminase from Nectria haematococca with inhibitor boundThe (R)-selective transaminase from Nectria haematococca with inhibitor bound
Structural highlights
Publication Abstract from PubMedDuring the last decade the use of transaminases for the production of pharmaceutical and fine chemical intermediates has attracted a great deal of attention. Transaminases are versatile biocatalysts for the efficient production of amine intermediates and many have (S)-enantiospecificity. Transaminases with (R)-specificity are needed to expand the applications of these enzymes in biocatalysis. In this work we have identified a fungal putative (R)-specific transaminase from the Eurotiomycetes Nectria haematococca, cloned a synthetic version of this gene, demonstrated (R)-selective deamination of several substrates including (R)-alpha-methylbenzylamine, as well as production of (R)-amines, and determined its crystal structure. The crystal structures of the holoenzyme and the complex with an inhibitor gabaculine offer the first detailed insight into the structural basis for substrate specificity and enantioselectivity of the industrially important class of (R)-selective amine:pyruvate transaminases. This article is protected by copyright. All rights reserved. STRUCTURED DIGITAL ABSTRACT: TAm and TAm bind by x-ray crystallography (View interaction). The substrate specificity, enantioselectivity and structure of the (R)-selective amine:pyruvate transaminase from Nectria haematococca.,Sayer C, Martinez-Torres RJ, Richter N, Isupov MN, Hailes HC, Littlechild JA, Ward JM FEBS J. 2014 Mar 11. doi: 10.1111/febs.12778. PMID:24618038[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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