7jso | pdb_00007jso

P. syringae AldA Indole-3-Acetaldehyde Dehydrogenase C302A mutant in complex with NAD+ and IAA

spinqualitylabelsall models 7jso, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7jso is a 8 chain structure with sequence from Pseudomonas syringae pv. tomato str. DC3000. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.848Å Ligands: IAC, NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q88BC5_PSESM Publication Abstract from PubMed Aldehyde dehydrogenases (ALDHs) catalyze the conversion of various aliphatic and aromatic aldehydes into corresponding carboxylic acids. Traditionally considered as housekeeping enzymes, new biochemical roles are being identified for members of ALDH family. Recent work showed that AldA from the plant pathogen Pseudomonas syringae strain PtoDC3000 (PtoDC3000) functions as an indole-3-acetaldehyde dehydrogenase for the synthesis of indole-3-acetic acid (IAA). IAA produced by AldA allows the pathogen to suppress salicylic acid-mediated defenses in the model plant Arabidopsis thaliana. Here we present a biochemical and structural analysis of the AldA indole-3-acetaldehyde dehydrogenase from PtoDC3000. Site-directed mutants targeting the catalytic residues Cys302 and Glu267 resulted in a loss of enzymatic activity. The X-ray crystal structure of the catalytically inactive AldA C302A mutant in complex with IAA and NAD+ showed the cofactor adopting a conformation that differs from the previously reported structure of AldA. These structures suggest that NAD+ undergoes a conformational change during the AldA reaction mechanism similar to that reported for human ALDH. Site-directed mutagenesis of the IAA binding site indicates that changes in the active site surface reduces AldA activity; however, substitution of Phe169 with a tryptophan altered the substrate selectivity of the mutant to prefer octanal. The present study highlights the inherent biochemical versatility of members of the ALDH enzyme superfamily in P. syringae. Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae PtoDC3000.,Zhang K, Lee JS, Liu R, Chan ZT, Dawson TJ, De Togni ES, Edwards CT, Eng IK, Gao AR, Goicouria LA, Hall EM, Hu KA, Huang K, Kizhner A, Kodama KC, Lin AZ, Liu JY, Lu AY, Peng OW, Ryu EP, Shi S, Sorkin ML, Walker PL, Wang GJ, Xu MC, Yang RS, Cascella B, Cruz W, Holland CK, McClerkin SA, Kunkel BN, Lee SG, Jez JM Biosci Rep. 2020 Dec 23;40(12). pii: 227102. doi: 10.1042/BSR20202959. PMID:33325526 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldehyde dehydrogenase 3D structures

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