4x2p: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4x2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X2P FirstGlance]. <br> | <table><tr><td colspan='2'>[[4x2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X2P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4x2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2p OCA], [https://pdbe.org/4x2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x2p RCSB], [https://www.ebi.ac.uk/pdbsum/4x2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x2p 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=4x2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2p OCA], [https://pdbe.org/4x2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x2p RCSB], [https://www.ebi.ac.uk/pdbsum/4x2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 06:39, 21 November 2024
P. putida mandelate racemase in complex with 3-hydroxypyruvateP. putida mandelate racemase in complex with 3-hydroxypyruvate
Structural highlights
FunctionPublication Abstract from PubMedMandelate racemase (MR), a member of the enolase superfamily, catalyzes the Mg(2+)-dependent interconversion of the enantiomers of mandelate. Several alpha-keto acids are modest competitive inhibitors of MR [e.g., mesoxalate (Ki = 1.8 +/- 0.3 mM) and 3-fluoropyruvate (Ki = 1.3 +/- 0.1 mM)], but, surprisingly, 3-hydroxypyruvate (3-HP) is an irreversible, time-dependent inhibitor (kinact/KI = 83 +/- 8 M(-1) s(-1)). Protection from inactivation by the competitive inhibitor benzohydroxamate, trypsinolysis and electrospray ionization tandem mass spectrometry analyses, and X-ray crystallographic studies reveal that 3-HP undergoes Schiff-base formation with Lys 166 at the active site, followed by formation of an aldehyde/enol(ate) adduct. Such a reaction is unprecedented in the enolase superfamily and may be a relic of an activity possessed by a promiscuous progenitor enzyme. The ability of MR to form and deprotonate a Schiff-base intermediate furnishes a previously unrecognized mechanistic link to other alpha/beta-barrel enzymes utilizing Schiff-base chemistry and is in accord with the sequence- and structure-based hypothesis that members of the metal-dependent enolase superfamily and the Schiff-base-forming N-acetylneuraminate lyase superfamily and aldolases share a common ancestor. Inactivation of Mandelate Racemase by 3-Hydroxypyruvate Reveals a Potential Mechanistic Link between Enzyme Superfamilies.,Nagar M, Wyatt BN, St Maurice M, Bearne SL Biochemistry. 2015 May 5;54(17):2747-57. doi: 10.1021/acs.biochem.5b00221. Epub, 2015 Apr 20. PMID:25844917[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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