4imp
From Proteopedia
(Difference between revisions)
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| - | + | ==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=''> | |
| - | + | == 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> | ||
| + | </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> | ||
| + | <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='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'>[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://www.rcsb.org/pdb/explore.do?structureId=4imp RCSB], [http://www.ebi.ac.uk/pdbsum/4imp PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:23489133</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Atcc 49460]] | [[Category: Atcc 49460]] | ||
| - | [[Category: Keatinge-Clay, A T | + | [[Category: Keatinge-Clay, A T]] |
| - | [[Category: Zheng, J | + | [[Category: Zheng, J]] |
[[Category: Dimerization element]] | [[Category: Dimerization element]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 12:02, 21 December 2014
The missing linker: a dimerization motif located within polyketide synthase modules
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