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| | ==The missing linker: a dimerization motif located within polyketide synthase modules== | | ==The missing linker: a dimerization motif located within polyketide synthase modules== |
| - | <StructureSection load='4imp' size='340' side='right' caption='[[4imp]], [[Resolution|resolution]] 2.57Å' scene=''> | + | <StructureSection load='4imp' size='340' side='right'caption='[[4imp]], [[Resolution|resolution]] 2.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4imp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49460 Atcc 49460]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IMP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IMP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4imp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_spinosa Saccharopolyspora spinosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IMP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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]] 2.57Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spnC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=60894 ATCC 49460])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </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=4imp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4imp OCA], [https://pdbe.org/4imp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4imp RCSB], [https://www.ebi.ac.uk/pdbsum/4imp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4imp ProSAT]</span></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=4imp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4imp OCA], [http://pdbe.org/4imp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4imp RCSB], [http://www.ebi.ac.uk/pdbsum/4imp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4imp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9ALM4_SACSN Q9ALM4_SACSN] |
| | <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: Atcc 49460]] | + | [[Category: Large Structures]] |
| - | [[Category: Keatinge-Clay, A T]] | + | [[Category: Saccharopolyspora spinosa]] |
| - | [[Category: Zheng, J]] | + | [[Category: Keatinge-Clay AT]] |
| - | [[Category: Dimerization element]] | + | [[Category: Zheng J]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9ALM4_SACSN
Publication Abstract from PubMed
The dimerization of multimodular polyketide synthases is essential for their function. Motifs that supplement the contacts made by dimeric polyketide synthase enzymes have previously been characterized outside the boundaries of modules, at the N- and C-terminal ends of polyketide synthase subunits. Here we describe a heretofore uncharacterized dimerization motif located within modules. The dimeric state of this dimerization element was elucidated through the 2.6 A resolution crystal structure of a fragment containing a dimerization element and a ketoreductase. The solution structure of a standalone dimerization element was revealed by nuclear magnetic resonance spectroscopy to be consistent with that of the crystal structure, and its dimerization constant was measured through analytical ultracentrifugation to be approximately 20 muM. The dimer buries approximately 990 A2 at its interface, and its C-terminal helices rigidly connect to ketoreductase domains to constrain their locations within a module. These structural restraints permitted the construction of a common type of polyketide synthase module.
The Missing Linker: A Dimerization Motif Located within Polyketide Synthase Modules.,Zheng J, Fage CD, Demeler B, Hoffman DW, Keatinge-Clay AT ACS Chem Biol. 2013 Mar 25. PMID:23489133[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zheng J, Fage CD, Demeler B, Hoffman DW, Keatinge-Clay AT. The Missing Linker: A Dimerization Motif Located within Polyketide Synthase Modules. ACS Chem Biol. 2013 Mar 25. PMID:23489133 doi:http://dx.doi.org/10.1021/cb400047s
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