6a4z: Difference between revisions
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==Oxidase ChaP== | ==Oxidase ChaP== | ||
<StructureSection load='6a4z' size='340' side='right' caption='[[6a4z]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='6a4z' size='340' side='right'caption='[[6a4z]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6a4z]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6a4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_chartreusis Streptomyces chartreusis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A4Z FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6a4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a4z OCA], [https://pdbe.org/6a4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a4z RCSB], [https://www.ebi.ac.uk/pdbsum/6a4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a4z ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4R0L3_STRCX Q4R0L3_STRCX] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces chartreusis]] | ||
[[Category: | [[Category: Ge HM]] | ||
[[Category: | [[Category: Zhang B]] | ||
Latest revision as of 12:41, 23 October 2024
Oxidase ChaPOxidase ChaP
Structural highlights
FunctionPublication Abstract from PubMedOxidative rearrangements play key roles in introducing structural complexity and biological activities of natural products biosynthesized by type II polyketide synthases (PKSs). Chartreusin (1) is a potent antitumor polyketide that contains a unique rearranged pentacyclic aromatic bilactone aglycone derived from a type II PKS. Herein, we report an unprecedented dioxygenase, ChaP, that catalyzes the final alpha-pyrone ring formation in 1 biosynthesis using flavin-activated oxygen as an oxidant. The X-ray crystal structures of ChaP and two homologues, docking studies, and site-directed mutagenesis provided insights into the molecular basis of the oxidative rearrangement that involves two successive C-C bond cleavage steps followed by lactonization. ChaP is the first example of a dioxygenase that requires a flavin-activated oxygen as a substrate despite lacking flavin binding sites, and represents a new class in the vicinal oxygen chelate enzyme superfamily. Molecular Basis for the Final Oxidative Rearrangement Steps in Chartreusin Biosynthesis.,Wang YS, Zhang B, Zhu J, Yang CL, Guo Y, Liu CL, Liu F, Huang H, Zhao S, Liang Y, Jiao RH, Tan RX, Ge HM J Am Chem Soc. 2018 Aug 15. doi: 10.1021/jacs.8b06623. PMID:30067334[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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