4ao4: Difference between revisions
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[[ | ==Structural Determinants of the beta-Selectivity of a Bacterial Aminotransferase== | ||
<StructureSection load='4ao4' size='340' side='right' caption='[[4ao4]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ao4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AO4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLK:(3R)-3-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]-5-METHYLHEXANOIC+ACID'>PLK</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yku|2yku]], [[2ykv|2ykv]], [[2ykx|2ykx]], [[2yky|2yky]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ao4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ao4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ao4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ao4 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: Crismaru, C G]] | |||
== | [[Category: Dijkstra, B W]] | ||
< | [[Category: Janssen, D B]] | ||
[[Category: Crismaru, C G | [[Category: Wybenga, G G]] | ||
[[Category: Dijkstra, B W | |||
[[Category: Janssen, D B | |||
[[Category: Wybenga, G G | |||
[[Category: Aminotransferase]] | [[Category: Aminotransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 14:34, 4 January 2015
Structural Determinants of the beta-Selectivity of a Bacterial Aminotransferase
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