2iwz: Difference between revisions

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-[[Image:2iwz.png|left|200px]]
-<!--
+==Human mitochondrial beta-ketoacyl ACP synthase complexed with hexanoic acid==
-The line below this paragraph, containing "STRUCTURE_2iwz", creates the "Structure Box" on the page.
+<StructureSection load='2iwz' size='340' side='right'caption='[[2iwz]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2iwz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWZ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6NA:HEXANOIC+ACID'>6NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
-{{STRUCTURE_2iwz|  PDB=2iwz  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwz OCA], [https://pdbe.org/2iwz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwz RCSB], [https://www.ebi.ac.uk/pdbsum/2iwz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/OXSM_HUMAN OXSM_HUMAN] May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.<ref>PMID:15668256</ref>
+== 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/iw/2iwz_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=2iwz ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Two distinct ways of organizing fatty acid biosynthesis exist: the multifunctional type I fatty acid synthase (FAS) of mammals, fungi, and lower eukaryotes with activities residing on one or two polypeptides; and the dissociated type II FAS of prokaryotes, plastids, and mitochondria with individual activities encoded by discrete genes. The beta-ketoacyl [ACP] synthase (KAS) moiety of the mitochondrial FAS (mtKAS) is targeted by the antibiotic cerulenin and possibly by the other antibiotics inhibiting prokaryotic KASes: thiolactomycin, platensimycin, and the alpha-methylene butyrolactone, C75. The high degree of structural similarity between mitochondrial and prokaryotic KASes complicates development of novel antibiotics targeting prokaryotic KAS without affecting KAS domains of cytoplasmic FAS. KASes catalyze the C(2) fatty acid elongation reaction using either a Cys-His-His or Cys-His-Asn catalytic triad. Three KASes with different substrate specificities participate in synthesis of the C(16) and C(18) products of prokaryotic FAS. By comparison, mtKAS carries out all elongation reactions in the mitochondria. We present the X-ray crystal structures of the Cys-His-His-containing human mtKAS and its hexanoyl complex plus the hexanoyl complex of the plant mtKAS from Arabidopsis thaliana. The structures explain (1) the bimodal (C(6) and C(10)-C(12)) substrate preferences leading to the C(8) lipoic acid precursor and long chains for the membranes, respectively, and (2) the low cerulenin sensitivity of the human enzyme; and (3) reveal two different potential acyl-binding-pocket extensions. Rearrangements taking place in the active site, including subtle changes in the water network, indicate a change in cooperativity of the active-site histidines upon primer binding.
-===HUMAN MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE COMPLEXED WITH HEXANOIC ACID===
+Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase.,Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A Protein Sci. 2007 Feb;16(2):261-72. PMID:17242430<ref>PMID:17242430</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2iwz" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17242430}}, adds the Publication Abstract to the page
+*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17242430 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17242430}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[2iwz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWZ OCA].
-==Reference==
-<ref group="xtra">PMID:17242430</ref><ref group="xtra">PMID:15668256</ref><references group="xtra"/>
-[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
 [[Category: Homo sapiens]]
-[[Category: Christensen, C E.]]
+[[Category: Large Structures]]
-[[Category: Henriksen, A.]]
+[[Category: Christensen CE]]
-[[Category: Kragelund, B B.]]
+[[Category: Henriksen A]]
-[[Category: Wettstein-Knowles, P Von.]]
+[[Category: Kragelund BB]]
-[[Category: Acyltransferase]]
+[[Category: Von Wettstein-Knowles P]]
-[[Category: Beta-ketoacyl acp synthase]]
-[[Category: Cerulenin]]
-[[Category: Claisen condensation]]
-[[Category: Fatty acid biosynthesis]]
-[[Category: Fatty acid synthesis]]
-[[Category: Homo sapien]]
-[[Category: Ka]]
-[[Category: Lipid synthesis]]
-[[Category: Mitochondria]]
-[[Category: Mitochondrion]]
-[[Category: Transferase]]
-[[Category: Transit peptide]]