5ecn
From Proteopedia
Crystal Structure of FIN219-FIP1 complex with JA, Leu and ATP
Structural highlights
FunctionJAR1_ARATH Catalyzes the synthesis of jasmonates-amino acid conjugates by adenylation; can use Ile and, in vitro at least, Val, Leu and Phe as conjugating amino acids on jasmonic acid (JA) and 9,10-dihydro-JA substrates, and to a lower extent, on 3-oxo-2-(2Z-pentenyl)-cyclopentane-1-butyric acid (OPC-4) and 12-hydroxy-JA (12-OH-JA). Can synthesize adenosine 5-tetraphosphate in vitro. Required for the JA-mediated signaling pathway that regulates many developmental and defense mechanisms, including growth root inhibition, vegetative storage proteins (VSPs) accumulation, induced systemic resistance (ISR), response to wounding and herbivores, tolerance to ozone O(3) (probably having a role in lesion containment). Plays an important role in the accumulation of JA-Ile in response to wounding, both locally and systemically; promotes JA responding genes especially in distal part of wounded plants, via the JA-Ile-stimulated degradation of JAZ repressor proteins by the SCF(COI)E3 ubiquitin-protein ligase pathway. Involved in the apoptosis-like programmed cell death (PCD) induced by fungal toxin fumonisin B1-mediated (FB1). Required for volatile compounds (C6-aldehydes and allo-ocimene)-mediated defense activation. Involved in the non-pathogenic rhizobacterium-mediated ISR (defense priming) by P.fluorescens (strains CHAOr and WCS417r) and P.putida LSW17S against infection leaf pathogens such as P.syringae pv. tomato and H.parasitica. Required for the JA-dependent resistance to fungi such as P.irregulare, U.vignae and U.appendiculatus. Necessary to induce systemic resistance against R.solanaceraum and P.syringae pv. tomato with P.oligandrum (a non-pathogenic biocontrol agent) cell wall protein fraction (CWP). Mediates PGIP2 accumulation in response to B.cinerea infection and thus contributes to resistance against this pathogen. Modulates the UV-B alteration of leaves attractiveness to diamondback moths P.xylostella leading to insect oviposition. Involved in the regulation of far-red light influence on development. Seems necessary for the salicylic acid (SA)-mediated, NPR1-independent resistance pathway. May contribute to the chitin-elicited pathway. Contributes to the sensitivity toward F.graminearum.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] Publication Abstract from PubMedFar-red (FR) light-coupled jasmonate (JA) signaling is necessary for plant defense and development. FR insensitive 219 (FIN219) is a member of the Gretchen Hagen 3 (GH3) family of proteins in Arabidopsis and belongs to the adenylate-forming family of enzymes. It directly controls biosynthesis of jasmonoyl-isoleucine in JA-mediated defense responses and interacts with FIN219-interacting protein 1 (FIP1) under FR light conditions. FIN219 and FIP1 are involved in FR light signaling and are regulators of the interplay between light and JA signaling. However, how their interactions affect plant physiological functions remains unclear. Here, we demonstrate the crystal structures of FIN219-FIP1 while binding with substrates at atomic resolution. Our results show an unexpected FIN219 conformation and demonstrate various differences between this protein and other members of the GH3 family. We show that the rotated C-terminal domain of FIN219 alters ATP binding and the core structure of the active site. We further demonstrate that this unique FIN219-FIP1 structure is crucial for increasing FIN219 activity and determines the priority of substrate binding. We suggest that the increased FIN219 activity resulting from the complex form, a conformation for domain switching, allows FIN219 to switch to its high-affinity mode and thereby enhances JA signaling under continuous FR light conditions. Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation.,Chen CY, Ho SS, Kuo TY, Hsieh HL, Cheng YS Proc Natl Acad Sci U S A. 2017 Feb 21. pii: 201609980. doi:, 10.1073/pnas.1609980114. PMID:28223489[27] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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