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5AJD

Not1 C-terminal domain in complex with Not4

Summary for 5AJD
Entry DOI10.2210/pdb5ajd/pdb
DescriptorCDC39P, GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 4 (2 entities in total)
Functional Keywordstranscription, ccr4-not, not1, not4
Biological sourceSACCHAROMYCES CEREVISIAE
More
Cellular locationCytoplasm : P34909
Total number of polymer chains12
Total formula weight433474.72
Authors
Bhaskar, V.,Basquin, J.,Conti, E. (deposition date: 2015-02-23, release date: 2015-04-29, Last modification date: 2024-01-10)
Primary citationBhaskar, V.,Basquin, J.,Conti, E.
Architecture of the Ubiquitylation Module of the Yeast Ccr4-not Complex.
Structure, 23:921-, 2015
Cited by
PubMed Abstract: The Ccr4-Not complex regulates eukaryotic gene expression at multiple levels, including mRNA turnover, translational repression, and transcription. We have studied the ubiquitylation module of the yeast Ccr4-Not complex and addressed how E3 ligase binds cognate E2 and how it is tethered to the complex. The 2.8-Å resolution crystal structure of the N-terminal RING domain of Not4 in complex with Ubc4 shows the detailed interactions of this E3-E2 complex. The 3.6-Å resolution crystal structure of the C-terminal domain of the yeast Not4 in complex with the C-terminal domain of Not1 reveals how a largely extended region at the C-terminus of Not4 wraps around a HEAT-repeat region of Not1. This C-terminal region of Not4 is only partly conserved in metazoans, rationalizing its weaker Not1-binding properties. The structural and biochemical data show how Not1 can incorporate both the ubiquitylation module and the Not2-Not3/5 module concomitantly in the Ccr4-Not complex.
PubMed: 25914052
DOI: 10.1016/J.STR.2015.03.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.62 Å)
Structure validation

237735

数据于2025-06-18公开中

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