5AIE

Not4 ring domain in complex with Ubc4

Summary for 5AIE

• Entry DOI: 10.2210/pdb5aie/pdb
• Descriptor: GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 4, UBIQUITIN-CONJUGATING ENZYME E2 4, ZINC ION (3 entities in total)
• Functional Keywords: ligase, signaling protein, not4 ring domain, ubc4, e2-e3 ligase
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm : P34909
• Total number of polymer chains: 2
• Total formula weight: 24281.15

Authors

Bhaskar, V.,Basquin, J.,Conti, E. (deposition date: 2015-02-12, release date: 2015-04-29, Last modification date: 2024-05-08)

Primary citation

Bhaskar, V.,Basquin, J.,Conti, E.
Architecture of the Ubiquitylation Module of the Yeast Ccr4-not Complex.
Structure, 23:921-, 2015

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)