6okf
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and C16-crypto Acyl Carrier Protein, AcpP== | ==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]]' scene=''> | + | <StructureSection load='6okf' size='340' side='right'caption='[[6okf]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == 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 [ | + | <table><tr><td colspan='2'>[[6okf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FABB_ECOLI FABB_ECOLI] 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. | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6okf" 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: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bartholow TG]] | [[Category: Bartholow TG]] | ||
Revision as of 07:12, 11 October 2023
Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and C16-crypto Acyl Carrier Protein, AcpP
| |||||||||||
