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[[ | ==Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase== | ||
<StructureSection load='2ykv' size='340' side='right' caption='[[2ykv]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ykv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_sp._luk Mesorhizobium sp. luk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKV OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IK2:4-DEOXY-4-ACETYLYAMINO-PYRIDOXAL-5-PHOSPHATE'>IK2</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yku|2yku]], [[2ykx|2ykx]], [[2yky|2yky]], [[4ao4|4ao4]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ykv RCSB], [http://www.ebi.ac.uk/pdbsum/2ykv PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chiral beta-amino acids occur as constituents of various natural and synthetic compounds with potentially useful bioactivities. The pyridoxal-5'-phosphate dependent (S)-selective transaminase from Mesorhizobium sp. LUK (MesAT) is a fold type I aminotransferase that can be used for the preparation of enantiopure beta-phenylalanine and derivatives thereof. Using X-ray crystallography, we solved structures of MesAT in complex with (S)-beta-phenylalanine, (R)-3-amino-5-methylhexanoic acid, 2-oxoglutarate, and the inhibitor 2-aminooxyacetic acid, which allowed us to unveil the basis of the amino acid specificity and enantioselectivity of this enzyme. The binding pocket of the side chain of a beta-amino acid is located on the 3'-O side of the PLP cofactor. The same binding pocket is utilized by MesAT to bind the alpha-carboxylate group of an alpha-amino acid. A beta-amino acid thus binds in a reverse orientation in the active site of MesAT as compared to an alpha-amino acid. Such a binding mode has not been reported before for any PLP-dependent aminotransferase and shows that the active site of MesAT has specifically evolved to accommodate both beta- and alpha-amino acids. | |||
Structural Determinants of the beta-Selectivity of a Bacterial Aminotransferase.,Wybenga GG, Crismaru CG, Janssen DB, Dijkstra BW J Biol Chem. 2012 Jun 28. PMID:22745123<ref>PMID:22745123</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Mesorhizobium sp. luk]] | [[Category: Mesorhizobium sp. luk]] | ||
[[Category: Crismaru, C G.]] | [[Category: Crismaru, C G.]] | ||
Revision as of 07:41, 14 May 2014
Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase
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