2fro

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:2fro.png|left|200px]]
 
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==MODEL OF THE BETA-CARBON PROCESSING ENZYMES AND ACYL CARRIER PROTEIN OF MODULAR POLYKETIDE SYNTHASES==
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The line below this paragraph, containing "STRUCTURE_2fro", creates the "Structure Box" on the page.
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<StructureSection load='2fro' size='340' side='right'caption='[[2fro]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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</table>
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{{STRUCTURE_2fro| PDB=2fro | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===MODEL OF THE BETA-CARBON PROCESSING ENZYMES AND ACYL CARRIER PROTEIN OF MODULAR POLYKETIDE SYNTHASES===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16564177}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2fro" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16564177 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16564177}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FRO OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:16564177</ref><references group="xtra"/>
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[[Category: Keatinge-Clay, A T]]
[[Category: Keatinge-Clay, A T]]
[[Category: Stroud, R M]]
[[Category: Stroud, R M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:24:02 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE BETA-CARBON PROCESSING ENZYMES AND ACYL CARRIER PROTEIN OF MODULAR POLYKETIDE SYNTHASES

PDB ID 2fro

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