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3kg7
From Proteopedia
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| - | {{STRUCTURE_3kg7| PDB=3kg7 | SCENE= }} | ||
| - | ===Dehydratase domain from CurH module of Curacin polyketide synthase=== | ||
| - | {{ABSTRACT_PUBMED_20152156}} | ||
| - | == | + | ==Dehydratase domain from CurH module of Curacin polyketide synthase== |
| - | [[3kg7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula Lyngbya majuscula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KG7 OCA]. | + | <StructureSection load='3kg7' size='340' side='right' caption='[[3kg7]], [[Resolution|resolution]] 2.77Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3kg7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula Lyngbya majuscula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KG7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kg6|3kg6]], [[3kg8|3kg8]], [[3kg9|3kg9]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">curH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158786 Lyngbya majuscula])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyacyl-[acyl-carrier-protein]_dehydratase 3-hydroxyacyl-[acyl-carrier-protein] dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.59 4.2.1.59] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg7 OCA], [http://pdbe.org/3kg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3kg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/kg/3kg7_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=3kg7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Modular polyketide synthases (PKS) make novel natural products through a series of preprogrammed chemical steps catalyzed by an assembly line of multidomain modules. Each assembly-line step involves unique extension and modification reactions, resulting in tremendous diversity of polyketide products. Dehydratase domains catalyze formation of an alpha,beta-double bond in the nascent polyketide intermediate. We present crystal structures of the four dehydratase domains from the curacin A PKS. The catalytic residues and substrate binding site reside in a tunnel within a single monomer. The positions of the catalytic residues and shape of the substrate tunnel explain how chirality of the substrate hydroxyl group may determine the configuration of the product double bond. Access to the active site may require opening the substrate tunnel, forming an open trench. The arrangement of monomers within the dimer is consistent among PKS dehydratases and differs from that seen in the related mammalian fatty acid synthases. | ||
| - | + | Crystal structures of dehydratase domains from the curacin polyketide biosynthetic pathway.,Akey DL, Razelun JR, Tehranisa J, Sherman DH, Gerwick WH, Smith JL Structure. 2010 Jan 13;18(1):94-105. PMID:20152156<ref>PMID:20152156</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3kg7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Lyngbya majuscula]] | [[Category: Lyngbya majuscula]] | ||
| - | [[Category: Akey, D L | + | [[Category: Akey, D L]] |
| - | [[Category: Smith, J L | + | [[Category: Smith, J L]] |
[[Category: Dehydratase]] | [[Category: Dehydratase]] | ||
[[Category: Double hotdog fold]] | [[Category: Double hotdog fold]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Polyketide synthase]] | [[Category: Polyketide synthase]] | ||
Current revision
Dehydratase domain from CurH module of Curacin polyketide synthase
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