View source for 4kgd


==High-resolution crystal structure of pyruvate oxidase from L. plantarum in complex with phosphate==
<StructureSection load='4kgd' size='340' side='right'caption='[[4kgd]], [[Resolution|resolution]] 1.06&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kgd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum_JDM1 Lactiplantibacillus plantarum JDM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGD 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]] 1.06&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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=4kgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgd OCA], [https://pdbe.org/4kgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgd RCSB], [https://www.ebi.ac.uk/pdbsum/4kgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgd ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Carbenes are highly reactive chemical compounds that are exploited as ligands in organometallic chemistry and are powerful organic catalysts. They were postulated to occur as transient intermediates in enzymes, yet their existence in a biological system could never be demonstrated directly. We present spectroscopic and structural data of a thiamin enzyme in a noncovalent complex with substrate, which implicate accumulation of a stable carbene as a major resonance contributor to deprotonated thiamin.

Observation of a stable carbene at the active site of a thiamin enzyme.,Meyer D, Neumann P, Ficner R, Tittmann K Nat Chem Biol. 2013 Jun 9. doi: 10.1038/nchembio.1275. PMID:23748673<ref>PMID:23748673</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kgd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Lactiplantibacillus plantarum JDM1]]
[[Category: Large Structures]]
[[Category: Neumann P]]
[[Category: Tittmann K]]