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| | <StructureSection load='2iwy' size='340' side='right'caption='[[2iwy]], [[Resolution|resolution]] 2.06Å' scene=''> | | <StructureSection load='2iwy' size='340' side='right'caption='[[2iwy]], [[Resolution|resolution]] 2.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iwy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IWY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iwy]] 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=2IWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c9h|2c9h]], [[2iwz|2iwz]], [[2ix4|2ix4]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwy OCA], [https://pdbe.org/2iwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwy RCSB], [https://www.ebi.ac.uk/pdbsum/2iwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwy ProSAT]</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=2iwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwy OCA], [http://pdbe.org/2iwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iwy RCSB], [http://www.ebi.ac.uk/pdbsum/2iwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwy ProSAT]</span></td></tr> | + | |
| | </table> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Christensen, C E]] | + | [[Category: Christensen CE]] |
| - | [[Category: Henriksen, A]] | + | [[Category: Henriksen A]] |
| - | [[Category: Kragelund, B B]] | + | [[Category: Kragelund BB]] |
| - | [[Category: Wettstein-Knowles, P von]] | + | [[Category: Von Wettstein-Knowles P]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[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]]
| + | |
| Structural highlights
Function
OXSM_HUMAN May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang L, Joshi AK, Hofmann J, Schweizer E, Smith S. Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain. J Biol Chem. 2005 Apr 1;280(13):12422-9. Epub 2005 Jan 24. PMID:15668256 doi:M413686200
- ↑ Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A. Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase. Protein Sci. 2007 Feb;16(2):261-72. PMID:17242430 doi:http://dx.doi.org/16/2/261
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