3kg8

<StructureSection load='3kg8' size='340' side='right' caption='[[3kg8]], [[Resolution|resolution]] 2.45&Aring;' scene=''>

<table><tr><td colspan='2'>[[3kg8]] is a 2 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=3KG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KG8 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kg6|3kg6]], [[3kg7|3kg7]], [[3kg9|3kg9]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">curJ ([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=3kg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg8 OCA], [http://pdbe.org/3kg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kg8 RCSB], [http://www.ebi.ac.uk/pdbsum/3kg8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg8 ProSAT]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/3kg8_consurf.spt"</scriptWhenChecked>

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== 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Akey, D L]]

[[Category: Smith, J L]]

[[Category: Polyketide synthase]]