PDBsum entry 4mn8

Transferase/transferase receptor

PDB id: 4mn8

Contents

Protein chains

759 a.a.

175 a.a.

21 a.a.

Ligands

NAG-NAG

NAG ×9

SO4 ×16

PDB id:

4mn8

Name:

Transferase/transferase receptor

Title:

Crystal structure of flg22 in complex with the fls2 and bak1 ectodomains

Structure:

Lrr receptor-like serine/threonine-protein kinase fls2. Chain: a. Fragment: fls2-lrr unp residues 25-800. Synonym: protein flagellin-sensing 2, protein flagellin-sensitive 2. Engineered: yes. Brassinosteroid insensitive 1-associated receptor kinase 1. Chain: b. Fragment: bak1-lrr unp residues 1-220. Synonym: atbak1, bri1-associated receptor kinase 1, protein

Source:

Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: fls2, at5g46330, mpl12.13, mpl12.8. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell: high five. Gene: bak1, elg, serk3, at4g33430, f17m5.190. Synthetic: yes.

Resolution:

3.06Å R-factor: 0.227 R-free: 0.275

Authors:

J.Chai,Y.Sun,Z.Han

Key ref:

Y.Sun et al. (2013). Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science, 342, 624-628. PubMed id: 24114786 DOI: 10.1126/science.1243825

Date:

10-Sep-13 Release date: 04-Dec-13

Protein chain

Q9FL28  (FLS2_ARATH) -  LRR receptor-like serine/threonine-protein kinase FLS2 from Arabidopsis thaliana

Seq: 1173 a.a.

Struc: 759 a.a.

Protein chain

Q94F62  (BAK1_ARATH) -  BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 from Arabidopsis thaliana

Seq: 615 a.a.

Struc: 175 a.a.

Protein chain

No UniProt id for this chain

Struc: 21 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, B: E.C.2.7.11.1 - non-specific serine/threonine 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⁺

L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + H(+)

L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + H(+)

• Enzyme class 3: Chain B: E.C.2.7.10.1 - receptor protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + 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: 10.1126/science.1243825

Science 342:624-628 (2013)

PubMed id: 24114786

Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.

Y.Sun, L.Li, A.P.Macho, Z.Han, Z.Hu, C.Zipfel, J.M.Zhou, J.Chai.

ABSTRACT

Flagellin perception in Arabidopsis is through recognition of its highly conserved N-terminal epitope (flg22) by flagellin-sensitive 2 (FLS2). Flg22 binding induces FLS2 heteromerization with BRASSINOSTEROID INSENSITIVE 1-associated kinase 1 (BAK1) and their reciprocal activation followed by plant immunity. Here, we report the crystal structure of FLS2 and BAK1 ectodomains complexed with flg22 at 3.06 angstroms. A conserved and a nonconserved site from the inner surface of the FLS2 solenoid recognize the C- and N-terminal segment of flg22, respectively, without oligomerization or conformational changes in the FLS2 ectodomain. Besides directly interacting with FLS2, BAK1 acts as a co-receptor by recognizing the C terminus of the FLS2-bound flg22. Our data reveal the molecular mechanisms underlying FLS2-BAK1 complex recognition of flg22 and provide insight into the immune receptor complex activation.