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3wgc

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==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==
==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==
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<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3wgc' size='340' side='right'caption='[[3wgc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_jandaei Aeromonas jandaei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene><br>
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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]] 2.5&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wgb|3wgb]]</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=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [https://pdbe.org/3wgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [https://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc ProSAT]</span></td></tr>
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<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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/LTAA_AERJA LTAA_AERJA] Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.
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== Publication Abstract from PubMed ==
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L-allo-Threonine aldolase (LATA), a pyridoxal-5'-phosphate-dependent enzyme from Aeromonas jandaei DK-39, stereospecifically catalyzes the reversible interconversion of L-allo-threonine to glycine and acetaldehyde. Here, the crystal structures of LATA and its mutant LATA_H128Y/S292R were determined at 2.59 and 2.50 A resolution, respectively. Their structures implied that conformational changes in the loop consisting of residues Ala123-Pro131, where His128 moved 4.2 A outwards from the active site on mutation to a tyrosine residue, regulate the substrate specificity for L-allo-threonine versus L-threonine. Saturation mutagenesis of His128 led to diverse stereoselectivity towards L-allo-threonine and L-threonine. Moreover, the H128Y mutant showed the highest activity towards the two substrates, with an 8.4-fold increase towards L-threonine and a 2.0-fold increase towards L-allo-threonine compared with the wild-type enzyme. The crystal structures of LATA and its mutant LATA_H128Y/S292R reported here will provide further insights into the regulation of the stereoselectivity of threonine aldolases targeted for the catalysis of L-allo-threonine/L-threonine synthesis.
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L-allo-Threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.,Qin HM, Imai FL, Miyakawa T, Kataoka M, Kitamura N, Urano N, Mori K, Kawabata H, Okai M, Ohtsuka J, Hou F, Nagata K, Shimizu S, Tanokura M Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1695-703. doi:, 10.1107/S1399004714007664. Epub 2014 May 30. PMID:24914980<ref>PMID:24914980</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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==See Also==
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</div>
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: L-allo-threonine aldolase]]
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[[Category: Aeromonas jandaei]]
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[[Category: Hou, F.]]
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[[Category: Large Structures]]
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[[Category: Imai, F L.]]
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[[Category: Hou F]]
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[[Category: Kataoka, M.]]
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[[Category: Imai FL]]
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[[Category: Miyakawa, T.]]
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[[Category: Kataoka M]]
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[[Category: Nagata, K.]]
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[[Category: Miyakawa T]]
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[[Category: Ohtsuka, J.]]
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[[Category: Nagata K]]
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[[Category: Okai, M.]]
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[[Category: Ohtsuka J]]
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[[Category: Qin, H M.]]
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[[Category: Okai M]]
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[[Category: Shimizu, S.]]
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[[Category: Qin HM]]
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[[Category: Tanokura, M.]]
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[[Category: Shimizu S]]
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[[Category: Lyase]]
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[[Category: Tanokura M]]
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[[Category: Pyridoxal-5'-phosphate]]
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[[Category: Threonine aldolase]]
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Current revision

Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant

PDB ID 3wgc

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