6avx
From Proteopedia
Crystal structure of Arabidopsis thaliana SOBER1 F65L
Structural highlights
Function[SOBR1_ARATH] Possesses carboxylesterase activity in vitro with a preference for short acyl chain substrates. Functions as a negative regulator of the hypersensitive response (HR) triggered by the bacterial type III effector protein AvrBsT (PubMed:17293566). Possesses phospholipase A2 (PLA2) activity and hydrolyzes phosphatidylcholine (PC), a lipid that is hydrolyzed by phospholipase D (PLD) to produce phosphatidic acid (PA). Required to suppress AvrBsT-dependent HR and PLD-dependent production of PA in response to AvrBsT elicitation (PubMed:19918071).[1] [2] Publication Abstract from PubMedSeveral Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related alpha/beta hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of alpha/beta hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1's biological function is not restricted to Arabidopsis thaliana and not limited to suppress HR induced by AvrBsT. A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors.,Burger M, Willige BC, Chory J Nat Commun. 2017 Dec 19;8(1):2201. doi: 10.1038/s41467-017-02347-w. PMID:29259199[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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