1ted

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[[Image:1ted.png|left|200px]]
 
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==Crystal structure of a type III polyketide synthase PKS18 from Mycobacterium tuberculosis==
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The line below this paragraph, containing "STRUCTURE_1ted", creates the "Structure Box" on the page.
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<StructureSection load='1ted' size='340' side='right'caption='[[1ted]], [[Resolution|resolution]] 2.25&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'>[[1ted]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TED 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]] 2.25&#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=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
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{{STRUCTURE_1ted| PDB=1ted | 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=1ted FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ted OCA], [https://pdbe.org/1ted PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ted RCSB], [https://www.ebi.ac.uk/pdbsum/1ted PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ted ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PKS18_MYCTU PKS18_MYCTU] Involved in the biosynthesis of tri- and tetraketide alpha-pyrones. Pks18 catalyzes the extension of medium- and long-chain aliphatic acyl-CoA substrates by using malonyl-CoA as an extender molecule to synthesize polyketide products.<ref>PMID:12941968</ref> <ref>PMID:15286723</ref> <ref>PMID:15984864</ref>
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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/te/1ted_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=1ted 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 superfamily of plant and bacterial type III polyketide synthases (PKSs) produces diverse metabolites with distinct biological functions. PKS18, a type III PKS from Mycobacterium tuberculosis, displays an unusual broad specificity for aliphatic long-chain acyl-coenzyme A (acyl-CoA) starter units (C(6)-C(20)) to produce tri- and tetraketide pyrones. The crystal structure of PKS18 reveals a 20 A substrate binding tunnel, hitherto unidentified in this superfamily of enzymes. This remarkable tunnel extends from the active site to the surface of the protein and is primarily generated by subtle changes of backbone dihedral angles in the core of the protein. Mutagenic studies combined with structure determination provide molecular insights into the structural elements that contribute to the chain length specificity of the enzyme. This first bacterial type III PKS structure underlines a fascinating example of the way in which subtle changes in protein architecture can generate metabolite diversity in nature.
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===Crystal structure of a type III polyketide synthase PKS18 from Mycobacterium tuberculosis===
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A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites.,Sankaranarayanan R, Saxena P, Marathe UB, Gokhale RS, Shanmugam VM, Rukmini R Nat Struct Mol Biol. 2004 Sep;11(9):894-900. Epub 2004 Aug 1. PMID:15286723<ref>PMID:15286723</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_15286723}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ted" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15286723 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15286723}}
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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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[[1ted]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TED OCA].
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Rukmini R]]
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==Reference==
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[[Category: Sankaranarayanan R]]
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<ref group="xtra">PMID:15286723</ref><ref group="xtra">PMID:15039574</ref><references group="xtra"/>
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[[Category: Shanmugam VM]]
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[[Category: Mycobacterium tuberculosis h37rv]]
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[[Category: Naringenin-chalcone synthase]]
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[[Category: Rukmini, R.]]
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[[Category: Sankaranarayanan, R.]]
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[[Category: Shanmugam, V M.]]
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[[Category: Substrate binding tunnel]]
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[[Category: Thiolase fold]]
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[[Category: Transferase]]
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Current revision

Crystal structure of a type III polyketide synthase PKS18 from Mycobacterium tuberculosis

PDB ID 1ted

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