4C0G

Structure of the NOT-box domain of human CNOT3

Summary for 4C0G

• Entry DOI: 10.2210/pdb4c0g/pdb
• Related: 4C0D 4C0F
• Descriptor: CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 3 (2 entities in total)
• Functional Keywords: gene regulation, deadenylation, mrna decay, ccr4-not, hydrolase, transcription
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm : O75175
• Total number of polymer chains: 6
• Total formula weight: 77027.54

Authors

Boland, A.,Chen, Y.,Raisch, T.,Jonas, S.,Izaurralde, E.,Weichenrieder, O. (deposition date: 2013-08-01, release date: 2013-10-09, Last modification date: 2024-10-23)

Primary citation

Boland, A.,Chen, Y.,Raisch, T.,Jonas, S.,Kuzuoglu-Ozturk, D.,Wohlbold, L.,Weichenrieder, O.,Izaurralde, E.
Structure and Assembly of the not Module of the Human Ccr4-not Complex
Nat.Struct.Mol.Biol., 20:1289-, 2013

PubMed Abstract: The CCR4-NOT deadenylase complex is a master regulator of translation and mRNA stability. Its NOT module orchestrates recruitment of the catalytic subunits to target mRNAs. We report the crystal structure of the human NOT module formed by the CNOT1, CNOT2 and CNOT3 C-terminal (-C) regions. CNOT1-C provides a rigid scaffold consisting of two perpendicular stacks of HEAT-like repeats. CNOT2-C and CNOT3-C heterodimerize through their SH3-like NOT-box domains. The heterodimer is stabilized and tightly anchored to the surface of CNOT1 through an unexpected intertwined arrangement of peptide regions lacking defined secondary structure. These assembly peptides mold onto their respective binding surfaces and form extensive interfaces. Mutagenesis of individual interfaces and perturbation of endogenous protein ratios cause defects in complex assembly and mRNA decay. Our studies provide a structural framework for understanding the recruitment of the CCR4-NOT complex to mRNA targets.

PubMed: 24121232
DOI: 10.1038/NSMB.2681

Experimental method

X-RAY DIFFRACTION (2.4 Å)