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==Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpP== | ==Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpP== | ||
<StructureSection load='5kof' size='340' side='right' caption='[[5kof]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='5kof' size='340' side='right'caption='[[5kof]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kof]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOF FirstGlance]. <br> | <table><tr><td colspan='2'>[[5kof]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6W5:[(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-[2-(prop-2-enoylamino)ethylamino]propyl]amino]butyl]+dihydrogen+phosphate'>6W5</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6W5:[(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-[2-(prop-2-enoylamino)ethylamino]propyl]amino]butyl]+dihydrogen+phosphate'>6W5</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='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> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FABB_ECOL6 FABB_ECOL6]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity). [[http://www.uniprot.org/uniprot/ACP_ECO45 ACP_ECO45]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | [[http://www.uniprot.org/uniprot/FABB_ECOL6 FABB_ECOL6]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity). [[http://www.uniprot.org/uniprot/ACP_ECO45 ACP_ECO45]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and beta-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli. | |||
Molecular basis for interactions between an acyl carrier protein and a ketosynthase.,Milligan JC, Lee DJ, Jackson DR, Schaub AJ, Beld J, Barajas JF, Hale JJ, Luo R, Burkart MD, Tsai SC Nat Chem Biol. 2019 Jul;15(7):669-671. doi: 10.1038/s41589-019-0301-y. Epub 2019 , Jun 17. PMID:31209348<ref>PMID:31209348</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5kof" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | |||
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | |||
[[Category: Barajas, J F]] | [[Category: Barajas, J F]] | ||
[[Category: Jackson, D R]] | [[Category: Jackson, D R]] | ||
Revision as of 09:08, 7 August 2019
Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpPCrosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpP
Structural highlights
Function[FABB_ECOL6] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity). [ACP_ECO45] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] Publication Abstract from PubMedFatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and beta-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli. Molecular basis for interactions between an acyl carrier protein and a ketosynthase.,Milligan JC, Lee DJ, Jackson DR, Schaub AJ, Beld J, Barajas JF, Hale JJ, Luo R, Burkart MD, Tsai SC Nat Chem Biol. 2019 Jul;15(7):669-671. doi: 10.1038/s41589-019-0301-y. Epub 2019 , Jun 17. PMID:31209348[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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