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2ykv

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<StructureSection load='2ykv' size='340' side='right'caption='[[2ykv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2ykv' size='340' side='right'caption='[[2ykv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ykv]] 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=2YKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ykv]] 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=2YKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKV FirstGlance]. <br>
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</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=IK2:4-DEOXY-4-ACETYLYAMINO-PYRIDOXAL-5-PHOSPHATE'>IK2</scene></td></tr>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yku|2yku]], [[2ykx|2ykx]], [[2yky|2yky]], [[4ao4|4ao4]]</div></td></tr>
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<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=IK2:4-DEOXY-4-ACETYLYAMINO-PYRIDOXAL-5-PHOSPHATE'>IK2</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=2ykv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykv OCA], [https://pdbe.org/2ykv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykv RCSB], [https://www.ebi.ac.uk/pdbsum/2ykv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykv ProSAT]</span></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=2ykv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykv OCA], [https://pdbe.org/2ykv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykv RCSB], [https://www.ebi.ac.uk/pdbsum/2ykv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A3EYF7_9HYPH A3EYF7_9HYPH]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ykv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mesorhizobium sp. luk]]
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[[Category: Mesorhizobium sp. LUK]]
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[[Category: Crismaru, C G]]
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[[Category: Crismaru CG]]
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[[Category: Dijkstra, B W]]
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[[Category: Dijkstra BW]]
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[[Category: Janssen, D B]]
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[[Category: Janssen DB]]
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[[Category: Wybenga, G G]]
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[[Category: Wybenga GG]]
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[[Category: Transferase]]
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Current revision

Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase

PDB ID 2ykv

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