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2z5l
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2z5l" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z5l, resolution 1.95Å" /> '''The first ketoreduct...) |
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| - | [[Image:2z5l.jpg|left|200px]]<br /><applet load="2z5l" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2z5l, resolution 1.95Å" /> | ||
| - | '''The first ketoreductase of the tylosin PKS'''<br /> | ||
| - | == | + | ==The first ketoreductase of the tylosin PKS== |
| - | + | <StructureSection load='2z5l' size='340' side='right'caption='[[2z5l]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2z5l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_fradiae Streptomyces fradiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z5L FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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=2z5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5l OCA], [https://pdbe.org/2z5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z5l RCSB], [https://www.ebi.ac.uk/pdbsum/2z5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z5l ProSAT]</span></td></tr> | |
| - | [ | + | </table> |
| - | [[ | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/O33954_STRFR O33954_STRFR] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z5/2z5l_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z5l ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Because it controls the majority of polyketide stereocenters, the ketoreductase (KR) is a central target in engineering polyketide synthases (PKSs). To elucidate the mechanisms of stereocontrol, the structure of KR from the first module of the tylosin PKS was determined. A comparison with a recently solved erythromycin KR that operates on the same substrate explains why their products have opposite alpha-substituent chiralities. The structure reveals how polyketides are guided into the active site by key residues in different KR types. There are four types of reductase-competent KRs, each capable of fixing a unique combination of alpha-substituent and beta-hydroxyl group chiralities, as well as two types of reductase-incompetent KRs that control alpha-substituent chirality alone. A protocol to assign how a module will enforce substituent chirality based on its sequence is presented. | ||
| - | + | A tylosin ketoreductase reveals how chirality is determined in polyketides.,Keatinge-Clay AT Chem Biol. 2007 Aug;14(8):898-908. PMID:17719489<ref>PMID:17719489</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2z5l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces fradiae]] | ||
| + | [[Category: Keatinge-Clay AT]] | ||
| + | [[Category: Stroud RM]] | ||
Current revision
The first ketoreductase of the tylosin PKS
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