5T2V
Crystal structure of MSMEG_6753 a putative betaketoacyl-ACP reductase
Summary for 5T2V
| Entry DOI | 10.2210/pdb5t2v/pdb |
| Descriptor | Oxidoreductase, short chain dehydrogenase/reductase family protein, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | fabg, mycobacterium, fatty acids, oxidoreductase |
| Biological source | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) |
| Total number of polymer chains | 1 |
| Total formula weight | 25628.78 |
| Authors | Blaise, M.,Van Wyk, N.,Baneres-Roquet, F.,Guerardel, Y.,Kremer, L. (deposition date: 2016-08-24, release date: 2017-02-15, Last modification date: 2024-01-17) |
| Primary citation | Blaise, M.,Van Wyk, N.,Baneres-Roquet, F.,Guerardel, Y.,Kremer, L. Binding of NADP(+) triggers an open-to-closed transition in a mycobacterial FabG beta-ketoacyl-ACP reductase. Biochem. J., 474:907-921, 2017 Cited by PubMed Abstract: The ketoacyl-acyl carrier protein (ACP) reductase FabG catalyzes the NADPH/NADH dependent reduction of β-ketoacyl-ACP substrates to β-hydroxyacyl-ACP products, the first reductive step in the fatty acid biosynthesis elongation cycle. FabG proteins are ubiquitous in bacteria and are part of the type II fatty acid synthase system. Mining the genome uncovered several putative FabG-like proteins. Among them, we identified MSMEG_6753 whose gene was found adjacent to , encoding a recently characterized enoyl-CoA dehydratase, and to , encoding another potential reductase. Recombinantly expressed and purified MSMEG_6753 exhibits ketoacyl reductase activity in the presence of acetoacetyl-CoA and NADPH. This activity was subsequently confirmed by functional complementation studies in a thermosensitive mutant. Furthermore, comparison of the and the NADP-bound MSMEG_6753 crystal structures showed that cofactor binding induces a closed conformation of the protein. A Δ deletion mutant could be generated in , indicating that this gene is dispensable for mycobacterial growth. Overall, these results showcase the diversity of FabG-like proteins in mycobacteria and new structural features regarding the catalytic mechanism of this important family of enzymes that may be of importance for the rational design of specific FabG inhibitors. PubMed: 28126742DOI: 10.1042/BCJ20161052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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