4mz0
From Proteopedia
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| - | + | ==Structure of a ketosynthase-acyltransferase di-domain from module CurL of the curacin A polyketide synthase== | |
| - | + | <StructureSection load='4mz0' size='340' side='right' caption='[[4mz0]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4mz0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula_3l Lyngbya majuscula 3l]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MZ0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4myy|4myy]], [[4myz|4myz]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYNGBM3L_74440 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=489825 Lyngbya majuscula 3L])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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=4mz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mz0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mz0 RCSB], [http://www.ebi.ac.uk/pdbsum/4mz0 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Modular type I polyketide synthases (PKSs) are versatile biosynthetic systems that initiate, successively elongate, and modify acyl chains. Intermediate transfer between modules is mediated via docking domains, which are attractive targets for PKS pathway engineering to produce natural product analogs. We identified a class 2 docking domain in cyanobacterial PKSs and determined crystal structures for two docking domain pairs, revealing a distinct class 2 docking strategy for promoting intermediate transfer. The selectivity of class 2 docking interactions, demonstrated in binding and biochemical assays, could be altered by mutagenesis. We determined the ideal fusion location for exchanging class 1 and class 2 docking domains and demonstrated effective polyketide chain transfer in heterologous modules. Thus, class 2 docking domains are tools for rational bioengineering of a broad range of PKSs containing either class 1 or 2 docking domains. | ||
| - | + | Cyanobacterial polyketide synthase docking domains: a tool for engineering natural product biosynthesis.,Whicher JR, Smaga SS, Hansen DA, Brown WC, Gerwick WH, Sherman DH, Smith JL Chem Biol. 2013 Nov 21;20(11):1340-51. doi: 10.1016/j.chembiol.2013.09.015. Epub , 2013 Oct 31. PMID:24183970<ref>PMID:24183970</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Smaga, S S | + | == References == |
| - | [[Category: Smith, J L | + | <references/> |
| - | [[Category: Whicher, J R | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Lyngbya majuscula 3l]] | ||
| + | [[Category: Smaga, S S]] | ||
| + | [[Category: Smith, J L]] | ||
| + | [[Category: Whicher, J R]] | ||
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Alpha/beta hydrolase fold]] | [[Category: Alpha/beta hydrolase fold]] | ||
Revision as of 18:42, 21 December 2014
Structure of a ketosynthase-acyltransferase di-domain from module CurL of the curacin A polyketide synthase
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