3pqb

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<StructureSection load='3pqb' size='340' side='right'caption='[[3pqb]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
<StructureSection load='3pqb' size='340' side='right'caption='[[3pqb]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pqb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_griseoflavus"_krainsky_1914 "actinomyces griseoflavus" krainsky 1914]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PQB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pqb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseoflavus Streptomyces griseoflavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PQB FirstGlance]. <br>
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</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=VGP:(1R)-1,4-ANHYDRO-6-DEOXY-1-[(6R)-8-ETHENYL-1,6-DIHYDROXY-10,12-DIMETHOXY-6H-DIBENZO[C,H]CHROMEN-4-YL]-D-GALACTITOL'>VGP</scene></td></tr>
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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]] 2.324&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pop|3pop]]</div></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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=VGP:(1R)-1,4-ANHYDRO-6-DEOXY-1-[(6R)-8-ETHENYL-1,6-DIHYDROXY-10,12-DIMETHOXY-6H-DIBENZO[C,H]CHROMEN-4-YL]-D-GALACTITOL'>VGP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gilR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35619 "Actinomyces griseoflavus" Krainsky 1914])</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=3pqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pqb OCA], [https://pdbe.org/3pqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pqb RCSB], [https://www.ebi.ac.uk/pdbsum/3pqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pqb 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=3pqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pqb OCA], [https://pdbe.org/3pqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pqb RCSB], [https://www.ebi.ac.uk/pdbsum/3pqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pqb ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7X2G7_9ACTN Q7X2G7_9ACTN]
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GilR is a recently identified oxidoreductase that catalyzes the terminal step of gilvocarcin V biosynthesis and is a unique enzyme that establishes the lactone core of the polyketide-derived gilvocarcin chromophore. Gilvocarcin-type compounds form a small distinct family of anticancer agents that are involved in both photo-activated DNA-alkylation and histone H3 cross-linking. High resolution crystal structures of apoGilR and GilR in complex with its substrate pregilvocarcin V reveals that GilR belongs to the small group of a relatively new type of the vanillyl-alcohol oxidase flavoprotein family characterized by bicovalently tethered cofactors. GilR was found as a dimer, with the bicovalently attached FAD cofactor mediated through His-65 and Cys-125. Subsequent mutagenesis and functional assays indicate that Tyr-445 may be involved in reaction catalysis and in mediating the covalent attachment of FAD, whereas Tyr-448 serves as an essential residue initiating the catalysis by swinging away from the active site to accommodate binding of the 6R-configured substrate and consequently abstracting the proton of the hydroxyl residue of the substrate hemiacetal 6-OH group. These studies lay the groundwork for future enzyme engineering to broaden the substrate specificity of this bottleneck enzyme of the gilvocarcin biosynthetic pathway for the development of novel anti-cancer therapeutics.
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The Crystal Structure and Mechanism of an Unusual Oxidoreductase, GilR, Involved in Gilvocarcin V Biosynthesis.,Noinaj N, Bosserman MA, Schickli MA, Piszczek G, Kharel MK, Pahari P, Buchanan SK, Rohr J J Biol Chem. 2011 Jul 1;286(26):23533-43. Epub 2011 May 10. PMID:21561854<ref>PMID:21561854</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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</div>
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<div class="pdbe-citations 3pqb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Actinomyces griseoflavus krainsky 1914]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bosserman, M A]]
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[[Category: Streptomyces griseoflavus]]
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[[Category: Buchanan, S K]]
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[[Category: Bosserman MA]]
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[[Category: Kharel, M K]]
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[[Category: Buchanan SK]]
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[[Category: Noinaj, N]]
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[[Category: Kharel MK]]
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[[Category: Rohr, J]]
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[[Category: Noinaj N]]
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[[Category: Schickli, M A]]
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[[Category: Rohr J]]
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[[Category: Covalently bound fad]]
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[[Category: Schickli MA]]
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[[Category: Fad binding protein]]
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[[Category: Oxidoreductase]]
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Revision as of 13:33, 1 March 2024

The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis

PDB ID 3pqb

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