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3NGQ

Crystal structure of the human CNOT6L nuclease domain

Summary for 3NGQ
Entry DOI10.2210/pdb3ngq/pdb
Related3NGN 3NGO
DescriptorCCR4-NOT transcription complex subunit 6-like, 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsalpha/beta sandwich fold, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q96LI5
Total number of polymer chains1
Total formula weight45406.31
Authors
Wang, H.,Morita, M.,Yang, W.,Bartlam, M.,Yamamoto, T.,Rao, Z. (deposition date: 2010-06-13, release date: 2010-07-28, Last modification date: 2024-03-20)
Primary citationWang, H.,Morita, M.,Yang, X.,Suzuki, T.,Yang, W.,Wang, J.,Ito, K.,Wang, Q.,Zhao, C.,Bartlam, M.,Yamamoto, T.,Rao, Z.
Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity.
Embo J., 2010
Cited by
PubMed Abstract: CCR4, an evolutionarily conserved member of the CCR4-NOT complex, is the main cytoplasmic deadenylase. It contains a C-terminal nuclease domain with homology to the endonuclease-exonuclease-phosphatase (EEP) family of enzymes. We have determined the high-resolution three-dimensional structure of the nuclease domain of CNOT6L, a human homologue of CCR4, by X-ray crystallography using the single-wavelength anomalous dispersion method. This first structure of a deadenylase belonging to the EEP family adopts a complete alpha/beta sandwich fold typical of hydrolases with highly conserved active site residues similar to APE1. The active site of CNOT6L should recognize the RNA substrate through its negatively charged surface. In vitro deadenylase assays confirm the critical active site residues and show that the nuclease domain of CNOT6L exhibits full Mg(2+)-dependent deadenylase activity with strict poly(A) RNA substrate specificity. To understand the structural basis for poly(A) RNA substrate binding, crystal structures of the CNOT6L nuclease domain have also been determined in complex with AMP and poly(A) DNA. The resulting structures suggest a molecular deadenylase mechanism involving a pentacovalent phosphate transition.
PubMed: 20628353
DOI: 10.1038/emboj.2010.152
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

238582

數據於2025-07-09公開中

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