PDBsum entry 3rgx

Transferase

PDB id: 3rgx

Contents

Protein chain

734 a.a.

Ligands

NAG-NAG-NAG

NAG-NAG ×3

NAG-NAG-NAG-NAG

NAG ×3

Waters ×90

PDB id:

3rgx

Name:

Transferase

Title:

Structural insight into brassinosteroid perception by bri1

Structure:

Protein brassinosteroid insensitive 1. Chain: a. Fragment: unp residues 23-784. Synonym: bri1, atbri1, brassinosteroid lrr receptor kinase. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: bri1, at4g39400, f23k16.30. Expression_system_cell_line: high-5. Other_details: invitrogentm

Resolution:

2.47Å R-factor: 0.202 R-free: 0.246

Authors:

J.Chai,Z.Han,J.She,J.Wang,W.Cheng,J.Wang

Key ref:

J.She et al. (2011). Structural insight into brassinosteroid perception by BRI1. Nature, 474, 472-476. PubMed id: 21666666

Date:

11-Apr-11 Release date: 15-Jun-11

Protein chain

O22476  (BRI1_ARATH) -  Protein BRASSINOSTEROID INSENSITIVE 1 from Arabidopsis thaliana

Seq: 1196 a.a.

Struc: 734 a.a.

Enzyme reactions

• Enzyme class 2: 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(+)

• Enzyme class 3: 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(+)

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

Nature 474:472-476 (2011)

PubMed id: 21666666

Structural insight into brassinosteroid perception by BRI1.

J.She, Z.Han, T.W.Kim, J.Wang, W.Cheng, J.Chang, S.Shi, J.Wang, M.Yang, Z.Y.Wang, J.Chai.

ABSTRACT

Brassinosteroids are essential phytohormones that have crucial roles in plant growth and development. Perception of brassinosteroids requires an active complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1 (BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1(LRR) in free and brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution independent of brassinolide. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, brassinolide binds to a hydrophobicity-dominating surface groove on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit mechanism involving stabilization of two interdomain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes brassinosteroids and provide insight into brassinosteroid-induced BRI1 activation.