1tqy

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{{Seed}}
 
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[[Image:1tqy.png|left|200px]]
 
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==The Actinorhodin Ketosynthase/Chain Length Factor==
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The line below this paragraph, containing "STRUCTURE_1tqy", creates the "Structure Box" on the page.
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<StructureSection load='1tqy' size='340' side='right'caption='[[1tqy]], [[Resolution|resolution]] 2.00&Aring;' 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'>[[1tqy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TQY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_1tqy| PDB=1tqy | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tqy OCA], [https://pdbe.org/1tqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tqy RCSB], [https://www.ebi.ac.uk/pdbsum/1tqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tqy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACTI1_STRCO ACTI1_STRCO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tq/1tqy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tqy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The synthesis of aromatic polyketides, such as actinorhodin, tetracycline and doxorubicin, begins with the formation of a polyketide chain. In type II polyketide synthases (PKSs), chains are polymerized by the heterodimeric ketosynthase-chain length factor (KS-CLF). Here we present the 2.0-A structure of the actinorhodin KS-CLF, which shows polyketides being elongated inside an amphipathic tunnel approximately 17 A in length at the heterodimer interface. The structure resolves many of the questions about the roles of KS and CLF. Although CLF regulates chain length, it does not have an active site; KS must catalyze both chain initiation and elongation. We provide evidence that the first cyclization of the polyketide occurs within the KS-CLF tunnel. The mechanistic details of this central PKS polymerase could guide biosynthetic chemists in designing new pharmaceuticals and polymers.
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===The Actinorhodin Ketosynthase/Chain Length Factor===
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An antibiotic factory caught in action.,Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM Nat Struct Mol Biol. 2004 Sep;11(9):888-93. Epub 2004 Aug 1. PMID:15286722<ref>PMID:15286722</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_15286722}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1tqy" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15286722 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15286722}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1TQY is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacteria Bacteria] and [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQY OCA].
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[[Category: Keatinge-Clay AT]]
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[[Category: Khosla C]]
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==Reference==
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[[Category: Maltby DA]]
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<ref group="xtra">PMID:15286722</ref><references group="xtra"/>
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[[Category: Medzihradszky KF]]
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[[Category: Bacteria]]
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[[Category: Stroud RM]]
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
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[[Category: Streptomyces coelicolor]]
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[[Category: Keatinge-Clay, A T.]]
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[[Category: Khosla, C.]]
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[[Category: Maltby, D A.]]
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[[Category: Medzihradszky, K F.]]
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[[Category: Stroud, R M.]]
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[[Category: Alpha-beta-alpha-beta-alpha]]
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[[Category: Heterodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:11:50 2009''
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Current revision

The Actinorhodin Ketosynthase/Chain Length Factor

PDB ID 1tqy

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