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| | <StructureSection load='5mso' size='340' side='right'caption='[[5mso]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='5mso' size='340' side='right'caption='[[5mso]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mso]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_marinum_M Mycobacterium marinum M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MSO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mso OCA], [http://pdbe.org/5mso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mso RCSB], [http://www.ebi.ac.uk/pdbsum/5mso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mso ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5mso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mso OCA], [https://pdbe.org/5mso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mso RCSB], [https://www.ebi.ac.uk/pdbsum/5mso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mso ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAR_MYCMM CAR_MYCMM]] Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes, by using ATP for energy to drive the reaction. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.<ref>PMID:23248280</ref> | + | [https://www.uniprot.org/uniprot/CAR_MYCMM CAR_MYCMM] Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes, by using ATP for energy to drive the reaction. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.<ref>PMID:23248280</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gahloth, D]] | + | [[Category: Mycobacterium marinum M]] |
| - | [[Category: Leys, D]] | + | [[Category: Gahloth D]] |
| - | [[Category: Adenylation domain]] | + | [[Category: Leys D]] |
| - | [[Category: Carboxylic acid reductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
CAR_MYCMM Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes, by using ATP for energy to drive the reaction. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.[1]
Publication Abstract from PubMed
Carboxylic acid reductase (CAR) catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes. The enzyme is related to the nonribosomal peptide synthetases, consisting of an adenylation domain fused via a peptidyl carrier protein (PCP) to a reductase termination domain. Crystal structures of the CAR adenylation-PCP didomain demonstrate that large-scale domain motions occur between the adenylation and thiolation states. Crystal structures of the PCP-reductase didomain reveal that phosphopantetheine binding alters the orientation of a key Asp, resulting in a productive orientation of the bound nicotinamide. This ensures that further reduction of the aldehyde product does not occur. Combining crystallography with small-angle X-ray scattering (SAXS), we propose that molecular interactions between initiation and termination domains are limited to competing PCP docking sites. This theory is supported by the fact that (R)-pantetheine can support CAR activity for mixtures of the isolated domains. Our model suggests directions for further development of CAR as a biocatalyst.
Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis.,Gahloth D, Dunstan MS, Quaglia D, Klumbys E, Lockhart-Cairns MP, Hill AM, Derrington SR, Scrutton NS, Turner NJ, Leys D Nat Chem Biol. 2017 Sep;13(9):975-981. doi: 10.1038/nchembio.2434. Epub 2017 Jul , 17. PMID:28719588[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Akhtar MK, Turner NJ, Jones PR. Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities. Proc Natl Acad Sci U S A. 2013 Jan 2;110(1):87-92. doi: 10.1073/pnas.1216516110. , Epub 2012 Dec 17. PMID:23248280 doi:http://dx.doi.org/10.1073/pnas.1216516110
- ↑ Gahloth D, Dunstan MS, Quaglia D, Klumbys E, Lockhart-Cairns MP, Hill AM, Derrington SR, Scrutton NS, Turner NJ, Leys D. Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis. Nat Chem Biol. 2017 Sep;13(9):975-981. doi: 10.1038/nchembio.2434. Epub 2017 Jul , 17. PMID:28719588 doi:http://dx.doi.org/10.1038/nchembio.2434
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