PDBsum entry 5ecm

Ligase/transferase

PDB id: 5ecm

Contents

Protein chains

569 a.a.

214 a.a.

Ligands

JAA ×2

LEU ×2

GSH ×4

Waters ×1660

PDB id:

5ecm

Name:

Ligase/transferase

Title:

Crystal structure of fin219-fip1 complex with ja and leu

Structure:

Jasmonic acid-amido synthetase jar1. Chain: a, d. Synonym: jasmonate-amino acid synthetase jar1,protein far-red insensitive 219,protein jasmonate resistant 1. Engineered: yes. Glutathione s-transferase u20. Chain: b, c, e, f. Synonym: atgstu20,fin219-interacting protein 1,gst class-tau member 20.

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: jar1, fin219, at2g46370, f11c10.6. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: gstu20, fip1, at1g78370, f3f9.11. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.233 R-free: 0.246

Authors:

C.Y.Chen,Y.S.Cheng

Key ref:

C.Y.Chen et al. (2017). Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation. Proc Natl Acad Sci U S A, 114, E1815. PubMed id: 28223489 DOI: 10.1073/pnas.1609980114

Date:

20-Oct-15 Release date: 02-Nov-16

Protein chains

Q9SKE2  (JAR1_ARATH) -  Jasmonoyl--L-amino acid synthetase JAR1 from Arabidopsis thaliana

Seq: 575 a.a.

Struc: 569 a.a.

Protein chains

Q8L7C9  (GSTUK_ARATH) -  Glutathione S-transferase U20 from Arabidopsis thaliana

Seq: 217 a.a.

Struc: 214 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, D: E.C.6.3.2.52 - jasmonoyl--L-amino acid ligase.
• Reaction: a jasmonate + an L-alpha-amino acid + ATP = a jasmonyl-L-amino acid + AMP + diphosphate + H⁺

jasmonate (Bound ligand (Het Group name = JAA) corresponds exactly) + L-alpha-amino acid + ATP = jasmonyl-L-amino acid + AMP + diphosphate + H(+)

• Enzyme class 3: Chains B, C, E, F: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

RX (Bound ligand (Het Group name = GSH) corresponds exactly) + glutathione = S-substituted glutathione + halide anion + H(+)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1073/pnas.1609980114

Proc Natl Acad Sci U S A 114:E1815 (2017)

PubMed id: 28223489

Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation.

C.Y.Chen, S.S.Ho, T.Y.Kuo, H.L.Hsieh, Y.S.Cheng.

ABSTRACT

Far-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.