6X9L
Crystal Structure of Aldehyde Dehydrogenase C (AldC) mutant (C291A) from Pseudomonas syringae in complexed with NAD+ and Octanal
Summary for 6X9L
| Entry DOI | 10.2210/pdb6x9l/pdb |
| Descriptor | Aldehyde dehydrogenase family protein, OCTANAL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | aldehyde dehydrogenase c, aldc, aliphatic aldehyde, oxidoreductase |
| Biological source | Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000) |
| Total number of polymer chains | 2 |
| Total formula weight | 105148.70 |
| Authors | |
| Primary citation | Lee, S.G.,Harline, K.,Abar, O.,Akadri, S.O.,Bastian, A.G.,Chen, H.S.,Duan, M.,Focht, C.M.,Groziak, A.R.,Kao, J.,Kottapalli, J.S.,Leong, M.C.,Lin, J.J.,Liu, R.,Luo, J.E.,Meyer, C.M.,Mo, A.F.,Pahng, S.H.,Penna, V.,Raciti, C.D.,Srinath, A.,Sudhakar, S.,Tang, J.D.,Cox, B.R.,Holland, C.K.,Cascella, B.,Cruz, W.,McClerkin, S.A.,Kunkel, B.N.,Jez, J.M. The plant pathogen enzyme AldC is a long-chain aliphatic aldehyde dehydrogenase. J.Biol.Chem., 295:13914-13926, 2020 Cited by PubMed Abstract: Aldehyde dehydrogenases are versatile enzymes that serve a range of biochemical functions. Although traditionally considered metabolic housekeeping enzymes because of their ability to detoxify reactive aldehydes, like those generated from lipid peroxidation damage, the contributions of these enzymes to other biological processes are widespread. For example, the plant pathogen strain DC3000 uses an indole-3-acetaldehyde dehydrogenase to synthesize the phytohormone indole-3-acetic acid to elude host responses. Here we investigate the biochemical function of AldC from DC3000. Analysis of the substrate profile of AldC suggests that this enzyme functions as a long-chain aliphatic aldehyde dehydrogenase. The 2.5 Å resolution X-ray crystal of the AldC C291A mutant in a dead-end complex with octanal and NAD reveals an apolar binding site primed for aliphatic aldehyde substrate recognition. Functional characterization of site-directed mutants targeting the substrate- and NAD(H)-binding sites identifies key residues in the active site for ligand interactions, including those in the "aromatic box" that define the aldehyde-binding site. Overall, this study provides molecular insight for understanding the evolution of the prokaryotic aldehyde dehydrogenase superfamily and their diversity of function. PubMed: 32796031DOI: 10.1074/jbc.RA120.014747 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.52 Å) |
Structure validation
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