6z4x
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the CAK complex form Chaetomium thermophilum bound to ATP-gamma-S== | |
| + | <StructureSection load='6z4x' size='340' side='right'caption='[[6z4x]], [[Resolution|resolution]] 2.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6z4x]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z4X FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.98Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6z4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z4x OCA], [https://pdbe.org/6z4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z4x RCSB], [https://www.ebi.ac.uk/pdbsum/6z4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z4x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G0SF48_CHATD G0SF48_CHATD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:33055219</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6z4x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chaetomium thermophilum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kisker C]] | ||
| + | [[Category: Kuper J]] | ||
| + | [[Category: Peissert S]] | ||
Current revision
Structure of the CAK complex form Chaetomium thermophilum bound to ATP-gamma-S
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