5mso
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP== | |
| + | <StructureSection load='5mso' size='340' side='right' caption='[[5mso]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/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> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28719588</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5mso" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Gahloth, D]] | [[Category: Gahloth, D]] | ||
| + | [[Category: Leys, D]] | ||
| + | [[Category: Adenylation domain]] | ||
| + | [[Category: Carboxylic acid reductase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 03:59, 30 August 2017
Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP
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