View source for 9hnf


==Beta-keto acid cleavage enzyme from Paracoccus denitrificans with bound acetoacetate and acetyl-CoA==
<StructureSection load='9hnf' size='340' side='right'caption='[[9hnf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hnf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HNF 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AAE:ACETOACETIC+ACID'>AAE</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9hnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hnf OCA], [https://pdbe.org/9hnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hnf RCSB], [https://www.ebi.ac.uk/pdbsum/9hnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hnf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A1B802_PARDP A1B802_PARDP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The direct reduction of CO(2) into one-carbon molecules is key to highly efficient biological CO(2)-fixation. However, this strategy is currently restricted to anaerobic organisms and low redox potentials. In this study, we introduce the CORE cycle, a synthetic metabolic pathway that converts CO(2) to formate at aerobic conditions and ambient CO(2) levels, using only NADPH as a reductant. Combining theoretical pathway design and analysis, enzyme bioprospecting and high-throughput screening, modular assembly and adaptive laboratory evolution, we realize the CORE cycle in vivo and demonstrate that the cycle supports growth of E. coli by supplementing C1-metabolism and serine biosynthesis from CO(2). We further analyze the theoretical potential of the CORE cycle as a new entry-point for carbon in photorespiration and autotrophy. Overall, our work expands the solution space for biological carbon reduction, offering a promising approach to enhance CO(2) fixation processes such as photosynthesis, and opening avenues for synthetic autotrophy.

Design and implementation of aerobic and ambient CO(2)-reduction as an entry-point for enhanced carbon fixation.,Satanowski A, Marchal DG, Perret A, Petit JL, Bouzon M, Doring V, Dubois I, He H, Smith EN, Pellouin V, Petri HM, Rainaldi V, Nattermann M, Burgener S, Paczia N, Zarzycki J, Heinemann M, Bar-Even A, Erb TJ Nat Commun. 2025 Apr 1;16(1):3134. doi: 10.1038/s41467-025-57549-4. PMID:40169551<ref>PMID:40169551</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9hnf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paracoccus denitrificans PD1222]]
[[Category: Erb TJ]]
[[Category: Marchal DG]]
[[Category: Zarzycki J]]