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| | <StructureSection load='4u3v' size='340' side='right'caption='[[4u3v]], [[Resolution|resolution]] 1.73Å' scene=''> | | <StructureSection load='4u3v' size='340' side='right'caption='[[4u3v]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u3v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U3V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u3v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U3V FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pksR, BSU17220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3v OCA], [http://pdbe.org/4u3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u3v RCSB], [http://www.ebi.ac.uk/pdbsum/4u3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u3v 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=4u3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3v OCA], [https://pdbe.org/4u3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u3v RCSB], [https://www.ebi.ac.uk/pdbsum/4u3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u3v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PKSR_BACSU PKSR_BACSU]] Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.<ref>PMID:17234808</ref> | + | [https://www.uniprot.org/uniprot/PKSR_BACSU PKSR_BACSU] Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.<ref>PMID:17234808</ref> |
| | <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: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gay, D C]] | + | [[Category: Gay DC]] |
| - | [[Category: Keatinge-Clay, A T]] | + | [[Category: Keatinge-Clay AT]] |
| - | [[Category: Spear, P J]] | + | [[Category: Spear PJ]] |
| - | [[Category: Double-hotdog]]
| + | |
| - | [[Category: Isomerase]]
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| - | [[Category: Polyketide]]
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| - | [[Category: Trans-at]]
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| Structural highlights
Function
PKSR_BACSU Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.[1]
Publication Abstract from PubMed
Many polyketide natural products exhibit invaluable medicinal properties, yet much remains to be understood regarding the machinery responsible for their biosynthesis. The recently discovered trans-acyltransferase polyketide synthases employ processing enzymes that catalyze modifications unique from those of the classical cis-acyltransferase polyketide synthases. The enoyl-isomerase domains of these megasynthases shift double bonds and are well-represented by an enzyme that helps forge the triene system within the antibiotic produced by the prototypical bacillaene synthase. This first crystal structure of an enoyl-isomerase, at 1.73 A resolution, not only revealed relationships between this class of enzymes and dehydratases but also guided an investigation into the mechanism of double bond migration. The catalytic histidine, positioned differently from that of dehydratases, was demonstrated to independently shuttle a proton between the gamma- and alpha-positions of the intermediate. This unprecedented mechanism highlights the catalytic diversity of divergent enzymes within trans-acyltransferase polyketide synthases.
A Double-Hotdog with a New Trick: Structure and Mechanism of the trans-Acyltransferase Polyketide Synthase Enoyl-isomerase.,Gay DC, Spear PJ, Keatinge-Clay AT ACS Chem Biol. 2014 Aug 14. PMID:25089587[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Butcher RA, Schroeder FC, Fischbach MA, Straight PD, Kolter R, Walsh CT, Clardy J. The identification of bacillaene, the product of the PksX megacomplex in Bacillus subtilis. Proc Natl Acad Sci U S A. 2007 Jan 30;104(5):1506-9. Epub 2007 Jan 18. PMID:17234808 doi:http://dx.doi.org/10.1073/pnas.0610503104
- ↑ Gay DC, Spear PJ, Keatinge-Clay AT. A Double-Hotdog with a New Trick: Structure and Mechanism of the trans-Acyltransferase Polyketide Synthase Enoyl-isomerase. ACS Chem Biol. 2014 Aug 14. PMID:25089587 doi:http://dx.doi.org/10.1021/cb500459b
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