4x19
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4x19 is ON HOLD until Paper Publication Authors: Thunnissen, A.M.W.H., Poddar, H. Description: Crystal structure of native 4-OT from Pseudomonas pu...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of native 4-OT from Pseudomonas putida mt-2 at 1.94 Angstrom== | |
| + | <StructureSection load='4x19' size='340' side='right'caption='[[4x19]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4x19]] is a 30 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=4X19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X19 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]] 1.944Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</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=4x19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x19 OCA], [https://pdbe.org/4x19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x19 RCSB], [https://www.ebi.ac.uk/pdbsum/4x19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x19 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/4OT1_PSEPU 4OT1_PSEPU] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.<ref>PMID:1339435</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme 4-oxalocrotonate tautomerase (4-OT), which has a catalytic N-terminal proline residue (Pro1), can promiscuously catalyze various carbon-carbon bond-forming reactions, including aldol condensation of acetaldehyde with benzaldehyde to yield cinnamaldehyde, and Michael-type addition of acetaldehyde to a wide variety of nitroalkenes to yield valuable gamma-nitroaldehydes. To gain insight into how 4-OT catalyzes these unnatural reactions, we carried out exchange studies in D2 O, and X-ray crystallography studies. The former established that H-D exchange within acetaldehyde is catalyzed by 4-OT and that the Pro1 residue is crucial for this activity. The latter showed that Pro1 of 4-OT had reacted with acetaldehyde to give an enamine species. These results provide evidence of the mechanism of the 4-OT-catalyzed aldol and Michael-type addition reactions in which acetaldehyde is activated for nucleophilic addition by Pro1-dependent formation of an enamine intermediate. | ||
| - | + | Evidence for the Formation of an Enamine Species during Aldol and Michael-type Addition Reactions Promiscuously Catalyzed by 4-Oxalocrotonate Tautomerase.,Poddar H, Rahimi M, Geertsema EM, Thunnissen AM, Poelarends GJ Chembiochem. 2015 Feb 26. doi: 10.1002/cbic.201402687. PMID:25728471<ref>PMID:25728471</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4x19" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas putida]] | ||
| + | [[Category: Poddar H]] | ||
| + | [[Category: Thunnissen AMWH]] | ||
Current revision
Crystal structure of native 4-OT from Pseudomonas putida mt-2 at 1.94 Angstrom
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