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7JV7

Crystal Structure of the yeast RNA Pol II CTD kinase CTDK-1 complex

Summary for 7JV7
Entry DOI10.2210/pdb7jv7/pdb
DescriptorCTD kinase subunit alpha, CTD kinase subunit beta, CTD kinase subunit gamma, ... (5 entities in total)
Functional Keywordscdk, kinase, transcription, transferase
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Total number of polymer chains3
Total formula weight113809.81
Authors
Xie, Y.,Ren, Y. (deposition date: 2020-08-20, release date: 2021-01-27, Last modification date: 2024-03-06)
Primary citationXie, Y.,Lord, C.L.,Clarke, B.P.,Ivey, A.L.,Hill, P.S.,McDonald, W.H.,Wente, S.R.,Ren, Y.
Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex.
Proc.Natl.Acad.Sci.USA, 118:-, 2021
Cited by
PubMed Abstract: The C-terminal domain (CTD) kinase I (CTDK-1) complex is the primary RNA Polymerase II (Pol II) CTD Ser2 kinase in budding yeast. CTDK-1 consists of a cyclin-dependent kinase (CDK) Ctk1, a cyclin Ctk2, and a unique subunit Ctk3 required for CTDK-1 activity. Here, we present a crystal structure of CTDK-1 at 1.85-Å resolution. The structure reveals that, compared to the canonical two-component CDK-cyclin system, the third component Ctk3 of CTDK-1 plays a critical role in Ctk1 activation by stabilizing a key element of CDK regulation, the T-loop, in an active conformation. In addition, Ctk3 contributes to the assembly of CTDK-1 through extensive interactions with both Ctk1 and Ctk2. We also demonstrate that CTDK-1 physically and genetically interacts with the serine/arginine-like protein Gbp2. Together, the data in our work reveal a regulatory mechanism of CDK complexes.
PubMed: 33431688
DOI: 10.1073/pnas.2019163118
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85055301184 Å)
Structure validation

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