6z4x

Structure of the CAK complex form Chaetomium thermophilum bound to ATP-gamma-S

spinqualitylabelsall models 6z4x, resolution 2.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6z4x is a 6 chain structure with sequence from Chaetomium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.98Å Ligands: AGS, CL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SF48_CHATD Publication Abstract from PubMed Cyclin-dependent kinase 7 (CDK7), Cyclin H, and the RING-finger protein MAT1 form the heterotrimeric CDK-activating kinase (CAK) complex which is vital for transcription and cell-cycle control. When associated with the general transcription factor II H (TFIIH) it activates RNA polymerase II by hyperphosphorylation of its C-terminal domain (CTD). In the absence of TFIIH the trimeric complex phosphorylates the T-loop of CDKs that control cell-cycle progression. CAK holds a special position among the CDK branch due to this dual activity and the dependence on two proteins for activation. We solved the structure of the CAK complex from the model organism Chaetomium thermophilum at 2.6-A resolution. Our structure reveals an intricate network of interactions between CDK7 and its two binding partners MAT1 and Cyclin H, providing a structural basis for the mechanism of CDK7 activation and CAK activity regulation. In vitro activity measurements and functional mutagenesis show that CDK7 activation can occur independent of T-loop phosphorylation and is thus exclusively MAT1-dependent by positioning the CDK7 T-loop in its active conformation. Structural basis for CDK7 activation by MAT1 and Cyclin H.,Peissert S, Schlosser A, Kendel R, Kuper J, Kisker C Proc Natl Acad Sci U S A. 2020 Oct 27;117(43):26739-26748. doi: , 10.1073/pnas.2010885117. Epub 2020 Oct 14. PMID:33055219 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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