PDBsum entry 3dak

Transferase

PDB id: 3dak

Contents

Protein chains

279 a.a. *

Ligands

ANP ×4

Metals

_MG ×4

Waters ×530

* Residue conservation analysis

PDB id:

3dak

Name:

Transferase

Title:

Crystal structure of domain-swapped osr1 kinase domain

Structure:

Serine/threonine-protein kinase osr1. Chain: a, b, c, d. Fragment: protein kinase domain, unp residues 6-295. Synonym: oxidative stress-responsive 1 protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Strain: 1-295. Gene: oxsr1, kiaa1101, osr1. Expressed in: escherichia coli.

Resolution:

2.25Å R-factor: 0.199 R-free: 0.267

Authors:

S.Lee,M.H.Cobb,E.J.Goldsmith

Key ref:

S.J.Lee et al. (2009). Crystal structure of domain-swapped STE20 OSR1 kinase domain. Protein Sci, 18, 304-313. PubMed id: 19177573 DOI: 10.1002/pro.27

Date:

29-May-08 Release date: 10-Feb-09

Protein chains

O95747  (OXSR1_HUMAN) -  Serine/threonine-protein kinase OSR1 from Homo sapiens

Seq: 527 a.a.

Struc: 279 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 = ANP) matches with 81.25% similarity) + ADP + H(+)

L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] (Bound ligand (Het Group name = ANP) matches with 81.25% similarity) + ADP + H(+)

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

reference

DOI no: 10.1002/pro.27

Protein Sci 18:304-313 (2009)

PubMed id: 19177573

Crystal structure of domain-swapped STE20 OSR1 kinase domain.

S.J.Lee, M.H.Cobb, E.J.Goldsmith.

ABSTRACT

OSR1 (oxidative stress-responsive-1) and SPAK (Ste20/Sps1-related proline/alanine-rich kinase) belong to the GCK-VI subfamily of Ste20 group kinases. OSR1 and SPAK are key regulators of NKCCs (Na(+)/K(+)/2Cl(-) cotransporters) and activated by WNK family members (with-no-lysine kinase), mutations of which are known to cause Gordon syndrome, an autosomal dominant form of inherited hypertension. The crystal structure of OSR1 kinase domain has been solved at 2.25 A. OSR1 forms a domain-swapped dimer in an inactive conformation, in which P+1 loop and alphaEF helix are swapped between dimer-related monomers. Structural alignment with nonswapped Ste20 TAO2 kinase indicates that the integrity of chemical interactions in the kinase domain is well preserved in the domain-swapped interfaces. The OSR1 kinase domain has now been added to a growing list of domain-swapped protein kinases recently reported, suggesting that the domain-swapping event provides an additional layer of complexity in regulating protein kinase activity.

Selected figure(s)

Figure 5.
Domain-swapped interface in OSR1 kinase domain. (A) Intersubunit interface between [alpha]EF and [alpha]F. Polar interaction between R279 and E196[prime prime or minute] is represented in red dotted line. Each subunit is rendered in blue and yellow. (B) Intersubunit cation-[pi] interaction between E219 and W192. E219 is from [alpha]F and W219 is from P+1 loop of the other subunit.

Figure 6.
D-K-T catalytic triad in TAO2 and OSR1. (A) D-K-T catalytic triad in TAO2 kinase. (B) D-K-T catalytic triad in domain-swapped OSR1 kinase.

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2009, 18, 304-313) copyright 2009.

Figures were selected by an automated process.