2fro
From Proteopedia
(Difference between revisions)
(New page: '''Theoretical Model''' The entry 2FRO is a Theoretical Model titled 'Model of the Beta-Carbon Processing Enzymes and Acyl Carrier Protein of Modular Polyketide Synthases'. [[Category:Th...) |
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| - | + | {{Theoretical_model}} | |
| - | + | ==MODEL OF THE BETA-CARBON PROCESSING ENZYMES AND ACYL CARRIER PROTEIN OF MODULAR POLYKETIDE SYNTHASES== | |
| + | <StructureSection load='2fro' size='340' side='right'caption='[[2fro]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FRO FirstGlance]. <br> | ||
| + | </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=2fro FirstGlance], [https://www.ebi.ac.uk/pdbsum/2fro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fro ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structure of the ketoreductase (KR) from the first module of the erythromycin synthase with NADPH bound was solved to 1.79 A resolution. The 51 kDa domain has two subdomains, each similar to a short-chain dehydrogenase/reductase (SDR) monomer. One subdomain has a truncated Rossmann fold and serves a purely structural role stabilizing the other subdomain, which catalyzes the reduction of the beta-carbonyl of a polyketide and possibly the epimerization of an alpha-substituent. The structure enabled us to define the domain boundaries of KR, the dehydratase (DH), and the enoylreductase (ER). It also constrains the three-dimensional organization of these domains within a module, revealing that KR does not make dimeric contacts across the 2-fold axis of the module. The quaternary structure elucidates how substrates are shuttled between the active sites of polyketide synthases (PKSs), as well as related fatty acid synthases (FASs), and suggests how domains can be swapped to make hybrid synthases that produce novel polyketides. | ||
| - | + | The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases.,Keatinge-Clay AT, Stroud RM Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:16564177<ref>PMID:16564177</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2fro" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Theoretical Model]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Keatinge-Clay, A T]] | ||
| + | [[Category: Stroud, R M]] | ||
Current revision
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MODEL OF THE BETA-CARBON PROCESSING ENZYMES AND ACYL CARRIER PROTEIN OF MODULAR POLYKETIDE SYNTHASES
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