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==Tri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester== | |||
<StructureSection load='6eqo' size='340' side='right'caption='[[6eqo]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6eqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter_sp._NAP1 Erythrobacter sp. NAP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EQO 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=6eqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqo OCA], [https://pdbe.org/6eqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eqo RCSB], [https://www.ebi.ac.uk/pdbsum/6eqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A3WE14_9SPHN A3WE14_9SPHN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cells must cope with toxic or reactive intermediates formed during metabolism. One coping strategy is to sequester reactions that produce such intermediates within specialized compartments or tunnels connecting different active sites. Here, we show that propionyl-CoA synthase (PCS), an approximately 400-kDa homodimer, three-domain fusion protein and the key enzyme of the 3-hydroxypropionate bi-cycle for CO2 fixation, sequesters its reactive intermediate acrylyl-CoA. Structural analysis showed that PCS forms a multicatalytic reaction chamber. Kinetic analysis suggested that access to the reaction chamber and catalysis are synchronized by interdomain communication. The reaction chamber of PCS features three active sites and has a volume of only 33 nm(3). As one of the smallest multireaction chambers described in biology, PCS may inspire the engineering of a new class of dynamically regulated nanoreactors. | |||
The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite.,Bernhardsgrutter I, Vogeli B, Wagner T, Peter DM, Cortina NS, Kahnt J, Bange G, Engilberge S, Girard E, Riobe F, Maury O, Shima S, Zarzycki J, Erb TJ Nat Chem Biol. 2018 Oct 29. pii: 10.1038/s41589-018-0153-x. doi:, 10.1038/s41589-018-0153-x. PMID:30374166<ref>PMID:30374166</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6eqo" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Girard | *[[Acetyl-CoA synthetase 3D structures|Acetyl-CoA synthetase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Erythrobacter sp. NAP1]] | |||
[[Category: Large Structures]] | |||
[[Category: Bernhardsgruetter I]] | |||
[[Category: Engilberge S]] | |||
[[Category: Erb TJ]] | |||
[[Category: Girard E]] | |||
[[Category: Shima S]] | |||
[[Category: Voegeli B]] | |||
[[Category: Wagner T]] | |||
[[Category: Zarzycki J]] | |||
Latest revision as of 15:21, 9 May 2024
Tri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate esterTri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester
Structural highlights
FunctionPublication Abstract from PubMedCells must cope with toxic or reactive intermediates formed during metabolism. One coping strategy is to sequester reactions that produce such intermediates within specialized compartments or tunnels connecting different active sites. Here, we show that propionyl-CoA synthase (PCS), an approximately 400-kDa homodimer, three-domain fusion protein and the key enzyme of the 3-hydroxypropionate bi-cycle for CO2 fixation, sequesters its reactive intermediate acrylyl-CoA. Structural analysis showed that PCS forms a multicatalytic reaction chamber. Kinetic analysis suggested that access to the reaction chamber and catalysis are synchronized by interdomain communication. The reaction chamber of PCS features three active sites and has a volume of only 33 nm(3). As one of the smallest multireaction chambers described in biology, PCS may inspire the engineering of a new class of dynamically regulated nanoreactors. The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite.,Bernhardsgrutter I, Vogeli B, Wagner T, Peter DM, Cortina NS, Kahnt J, Bange G, Engilberge S, Girard E, Riobe F, Maury O, Shima S, Zarzycki J, Erb TJ Nat Chem Biol. 2018 Oct 29. pii: 10.1038/s41589-018-0153-x. doi:, 10.1038/s41589-018-0153-x. PMID:30374166[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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