7JSO

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

7JSO の概要

• エントリーDOI: 10.2210/pdb7jso/pdb
• 分子名称: Aldehyde dehydrogenase family protein, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, 1H-INDOL-3-YLACETIC ACID (3 entities in total)
• 機能のキーワード: aldehyde dehydrogenase, auxin, oxidoreductase
• 由来する生物種: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 428707.10

構造登録者

Jez, J.M. (登録日: 2020-08-15, 公開日: 2021-06-23, 最終更新日: 2024-12-25)

主引用文献

Zhang, K.,Lee, J.S.,Liu, R.,Chan, Z.T.,Dawson, T.J.,De Togni, E.S.,Edwards, C.T.,Eng, I.K.,Gao, A.R.,Goicouria, L.A.,Hall, E.M.,Hu, K.A.,Huang, K.,Kizhner, A.,Kodama, K.C.,Lin, A.Z.,Liu, J.Y.,Lu, A.Y.,Peng, O.W.,Ryu, E.P.,Shi, S.,Sorkin, M.L.,Walker, P.L.,Wang, G.J.,Xu, M.C.,Yang, R.S.,Cascella, B.,Cruz, W.,Holland, C.K.,McClerkin, S.A.,Kunkel, B.N.,Lee, S.G.,Jez, J.M.
Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae PtoDC3000.
Biosci.Rep., 40:-, 2020

PubMed Abstract: 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.

PubMed: 33325526
DOI: 10.1042/BSR20202959

実験手法

X-RAY DIFFRACTION (2.848 Å)