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| | <StructureSection load='5vbx' size='340' side='right'caption='[[5vbx]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='5vbx' size='340' side='right'caption='[[5vbx]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vbx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vbx]] is a 3 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=5VBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VBX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acpS, dpj, b2563, JW2547 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Holo-[acyl-carrier-protein]_synthase Holo-[acyl-carrier-protein] synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.7 2.7.8.7] </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=5vbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vbx OCA], [https://pdbe.org/5vbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vbx RCSB], [https://www.ebi.ac.uk/pdbsum/5vbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vbx 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=5vbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vbx OCA], [http://pdbe.org/5vbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vbx RCSB], [http://www.ebi.ac.uk/pdbsum/5vbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vbx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACPS_ECOLI ACPS_ECOLI]] Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein.<ref>PMID:7559576</ref> | + | [https://www.uniprot.org/uniprot/ACPS_ECOLI ACPS_ECOLI] Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein.<ref>PMID:7559576</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barb, A W]] | + | [[Category: Barb AW]] |
| - | [[Category: Marcella, A M]] | + | [[Category: Marcella AM]] |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trimer]]
| + | |
| Structural highlights
Function
ACPS_ECOLI Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein.[1]
Publication Abstract from PubMed
The Escherichia coli holo-(acyl carrier protein) synthase (ACPS) catalyzes the coenzyme A-dependent activation of apo-ACPP to generate holo-(acyl carrier protein) (holo-ACPP) in an early step of fatty acid biosynthesis. E. coli ACPS is sufficiently different from the human fatty acid synthase to justify the development of novel ACPS-targeting antibiotics. Models of E. coli ACPS in unliganded and holo-ACPP-bound forms solved by X-ray crystallography to 2.05A and 4.10A, respectively, revealed ACPS bound three product holo-ACPP molecules to form a 3:3 hexamer. Solution NMR spectroscopy experiments validated the ACPS binding interface on holo-ACPP using chemical shift perturbations and by determining the relative orientation of holo-ACPP to ACPS by fitting residual dipolar couplings. The binding interface is organized to arrange contacts between positively charged ACPS residues and the holo-ACPP phosphopantetheine moiety, indicating product contains more stabilizing interactions than expected in the enzyme:substrate complex. Indeed, holo-ACPP bound the enzyme with greater affinity than the substrate, apo-ACPP, and with negative cooperativity. The first equivalent of holo-ACPP bound with a KD=62+/-13nM, followed by the binding of two more equivalents of holo-ACPP with KD=1.2+/-0.2muM. Cooperativity was not observed for apo-ACPP which bound with KD=2.4+/-0.1muM. Strong product binding and high levels of holo-ACPP in the cell identify a potential regulatory role of ACPS in fatty acid biosynthesis.
Structure, high affinity and negative cooperativity of the Escherichia coli holo-(acyl carrier protein):holo-(acyl carrier protein) synthase complex.,Marcella AM, Culbertson SJ, Shogren-Knaak MA, Barb AW J Mol Biol. 2017 Oct 17. pii: S0022-2836(17)30497-7. doi:, 10.1016/j.jmb.2017.10.015. PMID:29054754[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lambalot RH, Walsh CT. Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J Biol Chem. 1995 Oct 20;270(42):24658-61. PMID:7559576
- ↑ Marcella AM, Culbertson SJ, Shogren-Knaak MA, Barb AW. Structure, high affinity and negative cooperativity of the Escherichia coli holo-(acyl carrier protein):holo-(acyl carrier protein) synthase complex. J Mol Biol. 2017 Oct 17. pii: S0022-2836(17)30497-7. doi:, 10.1016/j.jmb.2017.10.015. PMID:29054754 doi:http://dx.doi.org/10.1016/j.jmb.2017.10.015
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