PDBsum entry 5ci6

Transferase

PDB id: 5ci6

Contents

Protein chains

335 a.a.

350 a.a.

Waters ×6

PDB id:

5ci6

Name:

Transferase

Title:

Crystal structure of arabidopsis thaliana mpk6

Structure:

Mitogen-activated protein kinase 6. Chain: a, b. Fragment: unp residues 29-395. Synonym: map kinase 6. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: mpk6, at2g43790, f18o19.10. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.00Å R-factor: 0.228 R-free: 0.272

Authors:

X.Qin,P.Li,Z.Chen,D.Ren

Key ref:

B.Wang et al. (2016). Analysis of crystal structure of Arabidopsis MPK6 and generation of its mutants with higher activity. Sci Rep, 6, 25646. PubMed id: 27160427 DOI: 10.1038/srep25646

Date:

11-Jul-15 Release date: 25-May-16

Protein chain

Q39026  (MPK6_ARATH) -  Mitogen-activated protein kinase 6 from Arabidopsis thaliana

Seq: 395 a.a.

Struc: 335 a.a.

Protein chain

Q39026  (MPK6_ARATH) -  Mitogen-activated protein kinase 6 from Arabidopsis thaliana

Seq: 395 a.a.

Struc: 350 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.2.7.11.24 - mitogen-activated protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

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

reference

DOI no: 10.1038/srep25646

Sci Rep 6:25646 (2016)

PubMed id: 27160427

Analysis of crystal structure of Arabidopsis MPK6 and generation of its mutants with higher activity.

B.Wang, X.Qin, J.Wu, H.Deng, Y.Li, H.Yang, Z.Chen, G.Liu, D.Ren.

ABSTRACT

Mitogen-activated protein kinase (MAPK) cascades, which are the highly conserved signalling modules in eukaryotic organisms, have been shown to play important roles in regulating growth, development, and stress responses. The structures of various MAPKs from yeast and animal have been solved, and structure-based mutants were generated for their function analyses, however, the structures of plant MAPKs remain unsolved. Here, we report the crystal structure of Arabidopsis MPK6 at a 3.0 Å resolution. Although MPK6 is topologically similar to ERK2 and p38, the structures of the glycine-rich loop, MAPK insert, substrate binding sites, and L16 loop in MPK6 show notable differences from those of ERK2 and p38. Based on the structural comparison, we constructed MPK6 mutants and analyzed their kinase activity both in vitro and in planta. MPK6(F364L) and MPK6(F368L) mutants, in which Phe364 and Phe368 in the L16 loop were changed to Leu, respectively, acquired higher intrinsic kinase activity and retained the normal MAPKK activation property. The expression of MPK6 mutants with basal activity is sufficient to induce camalexin biosynthesis; however, to induce ethylene and leaf senescence, the expression of MPK6 mutants with higher activity is required. The results suggest that these mutants can be used to analyze the specific biological functions of MPK6.