View source for 2yku


==Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase==
<StructureSection load='2yku' size='340' side='right'caption='[[2yku]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yku]] is a 3 chain structure with sequence from [https://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=2YKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yku OCA], [https://pdbe.org/2yku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yku RCSB], [https://www.ebi.ac.uk/pdbsum/2yku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yku ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A3EYF7_9HYPH A3EYF7_9HYPH] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yku" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mesorhizobium sp. LUK]]
[[Category: Crismaru CG]]
[[Category: Dijkstra BW]]
[[Category: Janssen DB]]
[[Category: Wybenga GG]]