View source for 9pep


==Crystal structure of holo-pvspha==
<StructureSection load='9pep' size='340' side='right'caption='[[9pep]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9pep]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Paecilomyces_variotii Paecilomyces variotii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PEP 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]] 1.92&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=9pep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pep OCA], [https://pdbe.org/9pep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pep RCSB], [https://www.ebi.ac.uk/pdbsum/9pep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pep ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyridoxal 5'-phosphate (PLP)-dependent enzymes are among the most versatile biocatalysts, yet transformations involving the Cgamma-nucleophilic vinylglycine quinonoid (VGQ) intermediate remain exceptionally rare. Understanding the untapped reactivity of VGQ could open new avenues for developing PLP-dependent biocatalysts. Here, we establish a biocatalytic platform that artificially accesses and exploits the reactivity of this high-energy intermediate. By reprogramming SphA, a PLP-dependent enzyme that natively catalyzes decarboxylative Claisen condensation, to generate VGQ in situ through facile decarboxylation of vinylaminomalonate, we enable a decarboxylative [3 + 2] annulation between vinylaminomalonate and electron-deficient alkenes. Crystallographic, computational, and mutagenesis studies reveal the key mechanistic features underlying this abiotic transformation. Our findings demonstrate the latent [3 + 2] annulating potential of VGQ and expand the catalytic repertoire of PLP-dependent enzymes, establishing a new strategy for the enzymatic construction of complex carbocyclic architectures.

Pyridoxal 5'-Phosphate-Dependent Enzymatic Decarboxylative Annulation.,Chai W, Luo S, Xi W, He X, Zhang T, Zou Y, Hai Y J Am Chem Soc. 2026 Mar 2. doi: 10.1021/jacs.5c20979. PMID:41769737<ref>PMID:41769737</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9pep" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paecilomyces variotii]]
[[Category: Hai Y]]
[[Category: He X]]