5c1j
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of native (reduced) CorB== | |
| + | <StructureSection load='5c1j' size='340' side='right'caption='[[5c1j]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5c1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corallococcus_coralloides Corallococcus coralloides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C1J 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]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=5c1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1j OCA], [https://pdbe.org/5c1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c1j RCSB], [https://www.ebi.ac.uk/pdbsum/5c1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c1j ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D7RK32_CORCK D7RK32_CORCK] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Corallopyronin A is a polyketide derived from the myxobacterium Corallococcus coralloides with potent antibiotic features. The gene cluster responsible for the biosynthesis of corallopyronin A has been described recently, and it was proposed that CorB acts as a ketosynthase to interconnect two polyketide chains in a rare head-to-head condensation reaction. We determined the structure of CorB, the interconnecting polyketide synthase, to high resolution and found that CorB displays a thiolase fold. Site-directed mutagenesis showed that the catalytic triad consisting of a cysteine, a histidine and an asparagine is crucial for catalysis, and that this triad shares similarities with the triad found in HMG-CoA synthases. We synthesized a substrate mimic to derivatize purified CorB and confirmed substrate attachment by ESI-MS. Structural analysis of the complex yielded an electron density-based model for the polyketide chain and showed that the unusually wide, T-shaped active site is able to accommodate two polyketides simultaneously. Our structural analysis provides a platform for understanding the unusual head-to-head polyketide-interconnecting reaction catalyzed by CorB. | ||
| - | + | Structural basis of head to head polyketide fusion by CorB.,Zocher G, Vilstrup J, Heine D, Hallab A, Goralski E, Hertweck C, Stahl M, Schaberle TF, Stehle T Chem Sci. 2015 Nov 13;6(11):6525-6536. doi: 10.1039/c5sc02488a. Epub 2015 Aug 6. PMID:28757960<ref>PMID:28757960</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5c1j" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Corallococcus coralloides]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Stehle T]] | ||
| + | [[Category: Vilstrup J]] | ||
| + | [[Category: Zocher G]] | ||
Current revision
Crystal Structure of native (reduced) CorB
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