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| | <StructureSection load='1w0i' size='340' side='right'caption='[[1w0i]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1w0i' size='340' side='right'caption='[[1w0i]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w0i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w0i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1w0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0i OCA], [https://pdbe.org/1w0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0i RCSB], [https://www.ebi.ac.uk/pdbsum/1w0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0i ProSAT]</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=1w0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0i OCA], [https://pdbe.org/1w0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0i RCSB], [https://www.ebi.ac.uk/pdbsum/1w0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/KASM_ARATH KASM_ARATH]] Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.<ref>PMID:17616510</ref>
| + | [https://www.uniprot.org/uniprot/KASM_ARATH KASM_ARATH] Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.<ref>PMID:17616510</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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Henriksen, A]] | + | [[Category: Henriksen A]] |
| - | [[Category: Olsen, J G]] | + | [[Category: Olsen JG]] |
| - | [[Category: Rasmussen, A V]] | + | [[Category: Rasmussen AV]] |
| - | [[Category: Wettstein-Knowles, P von]] | + | [[Category: Von Wettstein-Knowles P]] |
| - | [[Category: Condensing enzyme]]
| + | |
| - | [[Category: Fatty acid elongation]]
| + | |
| - | [[Category: Lipid metabolism]]
| + | |
| - | [[Category: Synthase]]
| + | |
| Structural highlights
Function
KASM_ARATH Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.[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
Mitochondrial fatty acid synthesis is catalyzed by a dissociated fatty acid synthase similar to those of plant plastids and bacteria. The crystal structure of a mitochondrial beta-ketoacyl-[acyl carrier protein] synthase (mtKAS), namely that from Arabidopsis thaliana, has been determined for the first time. This enzyme accomplishes the vital condensation steps in constructing fatty acid carbon skeletons. The product profile of mtKAS is unusual in that C8 and C(14-16) fatty acyl chains predominate. An enzyme architecture that likely is the basis for the observed bimodal profile of mtKAS products can be derived from the shape of the acyl binding pocket.
Structure of the mitochondrial beta-ketoacyl-[acyl carrier protein] synthase from Arabidopsis and its role in fatty acid synthesis.,Olsen JG, Rasmussen AV, von Wettstein-Knowles P, Henriksen A FEBS Lett. 2004 Nov 5;577(1-2):170-4. PMID:15527780[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ewald R, Kolukisaoglu U, Bauwe U, Mikkat S, Bauwe H. Mitochondrial protein lipoylation does not exclusively depend on the mtKAS pathway of de novo fatty acid synthesis in Arabidopsis. Plant Physiol. 2007 Sep;145(1):41-8. Epub 2007 Jul 6. PMID:17616510 doi:http://dx.doi.org/10.1104/pp.107.104000
- ↑ Olsen JG, Rasmussen AV, von Wettstein-Knowles P, Henriksen A. Structure of the mitochondrial beta-ketoacyl-[acyl carrier protein] synthase from Arabidopsis and its role in fatty acid synthesis. FEBS Lett. 2004 Nov 5;577(1-2):170-4. PMID:15527780 doi:10.1016/j.febslet.2004.10.007
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