1U5Q

Crystal Structure of the TAO2 Kinase Domain: Activation and Specifity of a Ste20p MAP3K

Summary for 1U5Q

• Entry DOI: 10.2210/pdb1u5q/pdb
• Related: 1U5R
• Descriptor: serine/threonine protein kinase TAO2, CALCIUM ION (3 entities in total)
• Functional Keywords: serine/threonine protein kinase, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasmic vesicle membrane; Multi-pass membrane protein (By similarity). Isoform 2: Cell projection, dendrite: Q9JLS3
• Total number of polymer chains: 2
• Total formula weight: 79901.09

Authors

Zhou, T.,Raman, M.,Gao, Y.,Earnest, S.,Chen, Z.,Machius, M.,Cobb, M.H.,Goldsmith, E.J. (deposition date: 2004-07-28, release date: 2004-10-12, Last modification date: 2024-10-30)

Primary citation

Zhou, T.,Raman, M.,Gao, Y.,Earnest, S.,Chen, Z.,Machius, M.,Cobb, M.H.,Goldsmith, E.J.
Crystal Structure of the TAO2 Kinase Domain; Activation and Specificity of a Ste20p MAP3K.
STRUCTURE, 12:1891-1900, 2004

PubMed 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.

PubMed: 15458637
DOI: 10.1016/j.str.2004.07.021

Experimental method

X-RAY DIFFRACTION (2.1 Å)