5ecn | pdb_00005ecn

Crystal Structure of FIN219-FIP1 complex with JA, Leu and ATP

spinqualitylabelsall models 5ecn, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ecn is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, GSH, JAA, LEU Related: 5ech, 5eci, 5eck, 5ecl, 5ecm, 5eco, 5ecp, 5ecq, 5ecr, 5ecs Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [JAR1_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. [GSTUK_ARATH] Exhibits glutathione-dependent thiol transferase activities. Can use glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. Involved in the regulation of far-red light influence on development. Publication Abstract from PubMed Acyl acid amido synthetases of the GH3 family act as critical prereceptor modulators of plant hormone action; however, the molecular basis for their hormone selectivity is unclear. Here, we report the crystal structures of benzoate-specific Arabidopsis thaliana AtGH3.12/PBS3 and jasmonic acid (JA)-specific AtGH3.11/JAR1. These structures, combined with biochemical analysis, define features for the conjugation of amino acids to diverse acyl acid substrates and highlight the importance of conformational changes in the C-terminal domain for catalysis. We also identify residues forming the acyl acid binding site across the GH3 family and residues critical for amino acid recognition. Our results demonstrate how a highly adaptable three-dimensional scaffold is used for the evolution of promiscuous activity across an enzyme family for modulation of plant signaling molecules. Structural Basis for Prereceptor Modulation of Plant Hormones by GH3 Proteins.,Westfall CS, Zubieta C, Herrmann J, Kapp U, Nanao MH, Jez JM Science. 2012 May 24. PMID:22628555 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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