2z5l: Difference between revisions

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New page: left|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 1.95&Aring;" />
'''The first ketoreductase of the tylosin PKS'''<br />


==About this Structure==
==The first ketoreductase of the tylosin PKS==
2Z5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_fradiae Streptomyces fradiae]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5L OCA].  
<StructureSection load='2z5l' size='340' side='right'caption='[[2z5l]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
[[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
== Structural highlights ==
[[Category: Single protein]]
<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]] 1.95&#8491;</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&reg;/PubMed&reg;, 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: Streptomyces fradiae]]
[[Category: Keatinge-Clay, A.T.]]
[[Category: Keatinge-Clay AT]]
[[Category: Stroud, R.M.]]
[[Category: Stroud RM]]
[[Category: polyketide synthase ketoreductase]]
[[Category: rossman fold]]
[[Category: short-chain dehydrogenase/reductase]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:55:00 2008''
Retrieved from "https://proteopedia.org/2z5l"