4yuf: Difference between revisions
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==Crystal Structure of CorB== | ==Crystal Structure of CorB== | ||
<StructureSection load='4yuf' size='340' side='right' caption='[[4yuf]], [[Resolution|resolution]] 1.54Å' scene=''> | <StructureSection load='4yuf' size='340' side='right'caption='[[4yuf]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yuf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YUF OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4yuf]] 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=4YUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YUF 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]] 1.54Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yuf OCA], [https://pdbe.org/4yuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yuf RCSB], [https://www.ebi.ac.uk/pdbsum/4yuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yuf ProSAT]</span></td></tr> | ||
</table> | </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> | |||
</div> | |||
<div class="pdbe-citations 4yuf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Corallococcus coralloides]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Stehle T]] | ||
[[Category: | [[Category: Vilstrup J]] | ||
[[Category: | [[Category: Zocher G]] | ||
Latest revision as of 14:34, 6 November 2024
Crystal Structure of CorBCrystal Structure of CorB
Structural highlights
FunctionPublication Abstract from PubMedCorallopyronin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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