PDBsum entry 4j0m

Transferase

PDB id: 4j0m

Contents

Protein chains

724 a.a.

Ligands

NAG-NAG ×7

NAG-NAG-BMA-MAN-MAN-MAN ×2

NAG ×4

BLD ×2

Waters ×411

PDB id:

4j0m

Name:

Transferase

Title:

Crystal structure of brl1 (lrr) in complex with brassinolide

Structure:

Serine/threonine-protein kinase bri1-like 1. Chain: a, b. Fragment: unp residues 25-758. Synonym: brassinosteroid insensitive 1-like protein 1. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress, thale-cress. Organism_taxid: 3702. Gene: brl1, at1g55610, f20n2.4. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

2.50Å R-factor: 0.190 R-free: 0.239

Authors:

J.Chai,J.She,Z.Han,B.Zhou

Key ref:

J.She et al. (2013). Structural basis for differential recognition of brassinolide by its receptors. Protein Cell, 4, 475-482. PubMed id: 23709366 DOI: 10.1007/s13238-013-3027-8

Date:

31-Jan-13 Release date: 24-Jul-13

Protein chains

Q9ZWC8  (BRL1_ARATH) -  Serine/threonine-protein kinase BRI1-like 1 from Arabidopsis thaliana

Seq: 1166 a.a.

Struc: 724 a.a.

Enzyme reactions

• Enzyme class: 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(+)

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

reference

DOI no: 10.1007/s13238-013-3027-8

Protein Cell 4:475-482 (2013)

PubMed id: 23709366

Structural basis for differential recognition of brassinolide by its receptors.

J.She, Z.Han, B.Zhou, J.Chai.

ABSTRACT

Brassinosteroids, a group of plant steroid hormones, regulate many aspects of plant growth and development. We and other have previously solved the crystal structures of BRI1(LRR) in complex with brassinolide, the most active brassinosteroid identified thus far. Although these studies provide a structural basis for the recognition of brassinolide by its receptor BRI1, it still remains poorly understood how the hormone differentiates among its conserved receptors. Here we present the crystal structure of the BRI1 homolog BRL1 in complex with brassinolide. The structure shows that subtle differences around the brassinolide binding site can generate a striking effect on its recognition by the BRI1 family of receptors. Structural comparison of BRL1 and BRI1 in their brassinolide-bound forms reveals the molecular basis for differential binding of brassinolide to its different receptors, which can be used for more efficient design of plant growth regulators for agricultural practice. On the basis of our structural studies and others' data, we also suggest possible mechanisms for the activation of BRI1 family receptors.