6okf: Difference between revisions
New page: '''Unreleased structure''' The entry 6okf is ON HOLD until Paper Publication Authors: Mindrebo, J.T., Kim, W.E., Bartholow, T.G., Chen, A., Davis, T.D., La Clair, J., Burkart, M.D., Noe... |
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==Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and C16-crypto Acyl Carrier Protein, AcpP== | |||
<StructureSection load='6okf' size='340' side='right'caption='[[6okf]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OKF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRJ:N-[2-(dodecanoylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide'>MRJ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6okf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6okf OCA], [https://pdbe.org/6okf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6okf RCSB], [https://www.ebi.ac.uk/pdbsum/6okf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6okf ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carbon-carbon bond forming reactions are essential transformations in natural product biosynthesis. During de novo fatty acid and polyketide biosynthesis, beta-ketoacyl-acyl carrier protein (ACP) synthases (KS), catalyze this process via a decarboxylative Claisen-like condensation reaction. KSs must recognize multiple chemically distinct ACPs and choreograph a ping-pong mechanism, often in an iterative fashion. Here, we report crystal structures of substrate mimetic bearing ACPs in complex with the elongating KSs from Escherichia coli, FabF and FabB, in order to better understand the stereochemical features governing substrate discrimination by KSs. Complemented by molecular dynamics (MD) simulations and mutagenesis studies, these structures reveal conformational states accessed during KS catalysis. These data taken together support a gating mechanism that regulates acyl-ACP binding and substrate delivery to the KS active site. Two active site loops undergo large conformational excursions during this dynamic gating mechanism and are likely evolutionarily conserved features in elongating KSs. | |||
Gating mechanism of elongating beta-ketoacyl-ACP synthases.,Mindrebo JT, Patel A, Kim WE, Davis TD, Chen A, Bartholow TG, La Clair JJ, McCammon JA, Noel JP, Burkart MD Nat Commun. 2020 Apr 7;11(1):1727. doi: 10.1038/s41467-020-15455-x. PMID:32265440<ref>PMID:32265440</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6okf" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Davis | *[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | ||
[[Category: | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Bartholow TG]] | |||
[[Category: Burkart MD]] | |||
[[Category: Chen A]] | |||
[[Category: Davis TD]] | |||
[[Category: Kim WE]] | |||
[[Category: La Clair J]] | |||
[[Category: Mindrebo JT]] | |||
[[Category: Noel JP]] | |||
Latest revision as of 14:15, 30 October 2024
Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and C16-crypto Acyl Carrier Protein, AcpPCrosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and C16-crypto Acyl Carrier Protein, AcpP
Structural highlights
Publication Abstract from PubMedCarbon-carbon bond forming reactions are essential transformations in natural product biosynthesis. During de novo fatty acid and polyketide biosynthesis, beta-ketoacyl-acyl carrier protein (ACP) synthases (KS), catalyze this process via a decarboxylative Claisen-like condensation reaction. KSs must recognize multiple chemically distinct ACPs and choreograph a ping-pong mechanism, often in an iterative fashion. Here, we report crystal structures of substrate mimetic bearing ACPs in complex with the elongating KSs from Escherichia coli, FabF and FabB, in order to better understand the stereochemical features governing substrate discrimination by KSs. Complemented by molecular dynamics (MD) simulations and mutagenesis studies, these structures reveal conformational states accessed during KS catalysis. These data taken together support a gating mechanism that regulates acyl-ACP binding and substrate delivery to the KS active site. Two active site loops undergo large conformational excursions during this dynamic gating mechanism and are likely evolutionarily conserved features in elongating KSs. Gating mechanism of elongating beta-ketoacyl-ACP synthases.,Mindrebo JT, Patel A, Kim WE, Davis TD, Chen A, Bartholow TG, La Clair JJ, McCammon JA, Noel JP, Burkart MD Nat Commun. 2020 Apr 7;11(1):1727. doi: 10.1038/s41467-020-15455-x. PMID:32265440[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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