PDBsum entry 1u5q

Transferase

PDB id: 1u5q

Contents

Protein chains

309 a.a. *

Metals

_CA ×2

Waters ×434

* Residue conservation analysis

PDB id:

1u5q

Name:

Transferase

Title:

Crystal structure of the tao2 kinase domain: activation and specifity of a ste20p map3k

Structure:

Serine/threonine protein kinase tao2. Chain: a, b. Fragment: n-terminal kinase domain. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: serine/threonine protein kinase tao2. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.

Resolution:

2.10Å R-factor: 0.223 R-free: 0.269

Authors:

T.Zhou,M.Raman,Y.Gao,S.Earnest,Z.Chen,M.Machius,M.H.Cobb, E.J.Goldsmith

Key ref:

T.Zhou et al. (2004). Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K. Structure, 12, 1891-1900. PubMed id: 15458637 DOI: 10.1016/j.str.2004.07.021

Date:

28-Jul-04 Release date: 12-Oct-04

Protein chains

Q9JLS3  (TAOK2_RAT) -  Serine/threonine-protein kinase TAO2 from Rattus norvegicus

Seq: 1235 a.a.

Struc: 309 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⁺

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

reference

DOI no: 10.1016/j.str.2004.07.021

Structure 12:1891-1900 (2004)

PubMed id: 15458637

Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K.

T.Zhou, M.Raman, Y.Gao, S.Earnest, Z.Chen, M.Machius, M.H.Cobb, E.J.Goldsmith.

ABSTRACT

TAO2 is a mitogen-activated protein kinase kinase kinase (MAP3K) that doubly phosphorylates and activates the MAP kinase kinases (MAP2Ks) MEK3 and MEK6. The structure of the kinase domain of TAO2 (1-320) has been solved in its phosphorylated active conformation. The structure, together with structure-based mutagenic analysis, reveals that positively charged residues in the substrate binding groove mediate the first step in the dual phosphorylation of MEK6, on the threonine residue in the motif DS*VAKT*I (*denotes phosphorylation site) of MEK6. TAO2 is a Ste20p homolog, and the structure of active TAO2, in comparison with that of low-activity p21-activated protein kinase (PAK1), a Ste20p-related MAP4K, reveals how this group of kinases is activated by phosphorylation. Finally, active TAO2 displays unusual interactions with ATP, involving, in part, a subgroup-specific C-terminal extension of TAO2. The observed interactions may be useful in making specific inhibitors of TAO kinases.

Selected figure(s)

Figure 1.
Figure 1. Overall Structure and Electron Density of TAO2 Kinase Domain(A) Ribbon diagram of TAO2 (1-320) in complex with MgATP. Phosphate binding ribbon is colored yellow, catalytic loop is orange, and activation loop is pink. b strands are green, conserved helices are blue, and additional helices are purple (aA and aB) or magenta (aJ and aK). pSer181 and MgATP molecules are shown in ball-and-stick representation.(B) Electron density of apo-TAO2 in the vicinity of the pSer181 and the P+1 pocket, contoured at 1.0 s and drawn on O (Jones et al., 1991). Phosphate atom is green, and ordered water molecules are red spheres. Figure 1, Figure 3, Figure 4, Figure 5 and Figure 6 were prepared using Molscript (Kraulis, 1991) and rendered using POV-Ray (Persistence of Vision Ray Tracer v3.1g, POV-Team).

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 1891-1900) copyright 2004.

Figure was selected by an automated process.