4EC9

Crystal structure of full-length cdk9 in complex with cyclin t

Summary for 4EC9

• Entry DOI: 10.2210/pdb4ec9/pdb
• Related: 4EC8
• Descriptor: Cyclin-dependent kinase 9, Cyclin-T1 (2 entities in total)
• Functional Keywords: cyclin dependent kinase, cyclin, kinase, phosphorylation, nuclear, transferase-protein binding complex, transferase/protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P50750 O60563
• Total number of polymer chains: 2
• Total formula weight: 73059.87

Authors

Baumli, S.,Hole, A.J.,Endicott, J.A. (deposition date: 2012-03-26, release date: 2012-09-12, Last modification date: 2024-10-16)

Primary citation

Baumli, S.,Hole, A.J.,Wang, L.Z.,Noble, M.E.,Endicott, J.A.
The CDK9 tail determines the reaction pathway of positive transcription elongation factor b.
Structure, 20:1788-1795, 2012

PubMed Abstract: CDK9, the kinase of positive transcription elongation factor b (P-TEFb), stimulates transcription elongation by phosphorylating RNA polymerase II and transcription elongation factors. Using kinetic analysis of a human P-TEFb complex consisting of CDK9 and cyclin T, we show that the CDK9 C-terminal tail sequence is important for the catalytic mechanism and imposes an ordered binding of substrates and release of products. Crystallographic analysis of a CDK9/cyclin T complex in which the C-terminal tail partially blocks the ATP binding site reveals a possible reaction intermediate. Biochemical characterization of CDK9 mutants supports a model in which the CDK9 tail cycles through different conformational states. We propose that this mechanism is critical for the pattern of CTD Ser2 phosphorylation on actively transcribed genes.

PubMed: 22959624
DOI: 10.1016/j.str.2012.08.011

Experimental method

X-RAY DIFFRACTION (3.21 Å)