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5Z9X

Arabidopsis SMALL RNA DEGRADING NUCLEASE 1 in complex with an RNA substrate

Summary for 5Z9X
Entry DOI10.2210/pdb5z9x/pdb
DescriptorSmall RNA degrading nuclease 1, RNA (5'-R(P*GP*CP*CP*CP*AP*UP*UP*AP*G)-3'), SULFATE ION, ... (5 entities in total)
Functional Keywordsexonuclease, microrna turnover, protein-rna complex, plant protein, plant protein-rna complex, plant protein/rna
Biological sourceArabidopsis thaliana (Mouse-ear cress)
More
Total number of polymer chains2
Total formula weight49830.75
Authors
Chen, J.,Liu, L.,You, C.,Gu, J.,Ruan, W.,Zhang, L.,Gan, J.,Cao, C.,Huang, Y.,Chen, X.,Ma, J. (deposition date: 2018-02-05, release date: 2018-06-27, Last modification date: 2024-04-03)
Primary citationChen, J.,Liu, L.,You, C.,Gu, J.,Ruan, W.,Zhang, L.,Gan, J.,Cao, C.,Huang, Y.,Chen, X.,Ma, J.
Structural and biochemical insights into small RNA 3' end trimming by Arabidopsis SDN1.
Nat Commun, 9:3585-3585, 2018
Cited by
PubMed Abstract: A family of DEDDh 3'→5' exonucleases known as Small RNA Degrading Nucleases (SDNs) initiates the turnover of ARGONAUTE1 (AGO1)-bound microRNAs in Arabidopsis by trimming their 3' ends. Here, we report the crystal structure of Arabidopsis SDN1 (residues 2-300) in complex with a 9 nucleotide single-stranded RNA substrate, revealing that the DEDDh domain forms rigid interactions with the N-terminal domain and binds 4 nucleotides from the 3' end of the RNA via its catalytic pocket. Structural and biochemical results suggest that the SDN1 C-terminal domain adopts an RNA Recognition Motif (RRM) fold and is critical for substrate binding and enzymatic processivity of SDN1. In addition, SDN1 interacts with the AGO1 PAZ domain in an RNA-independent manner in vitro, enabling it to act on AGO1-bound microRNAs. These extensive structural and biochemical studies may shed light on a common 3' end trimming mechanism for 3'→5' exonucleases in the metabolism of small non-coding RNAs.
PubMed: 30181559
DOI: 10.1038/s41467-018-05942-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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數據於2024-11-06公開中

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