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PDBsum entry 5guh

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protein dna_rna metals links
Hydrolase/RNA PDB id
5guh

 

 

 

 

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Contents
Protein chain
759 a.a.
DNA/RNA
Metals
_MG ×2
Waters ×84
PDB id:
5guh
Name: Hydrolase/RNA
Title: Crystal structure of silkworm piwi-clade argonaute siwi bound to pirna
Structure: Piwi. Chain: a. Synonym: piwi,siwi,uncharacterized protein. Other_details: the n-terminal region (residues 1-129) was truncated by thermolysin treatment.. RNA (28-mer). Chain: b. Other_details: the bound rnas are co-purified endogenous pirnas, which have divergent sequences and lengths.
Source: Bombyx mori. Silk moth. Organism_taxid: 7091. Organism_taxid: 7091
Resolution:
2.40Å     R-factor:   0.211     R-free:   0.236
Authors: N.Matsumoto,H.Nishimasu,R.Ishitani,O.Nureki
Key ref: N.Matsumoto et al. (2016). Crystal Structure of Silkworm PIWI-Clade Argonaute Siwi Bound to piRNA. Cell, 167, 484. PubMed id: 27693359
Date:
29-Aug-16     Release date:   19-Oct-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A8D8P8  (SIWI_BOMMO) -  Piwi-like protein Siwi from Bombyx mori
Seq:
Struc:
 
Seq:
Struc:
899 a.a.
759 a.a.
Key:    PfamA domain  Secondary structure

DNA/RNA chain
  U-A-U-U-U-U-U-OMU 8 bases

 Enzyme reactions 
   Enzyme class: E.C.3.1.26.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Cell 167:484 (2016)
PubMed id: 27693359  
 
 
Crystal Structure of Silkworm PIWI-Clade Argonaute Siwi Bound to piRNA.
N.Matsumoto, H.Nishimasu, K.Sakakibara, K.M.Nishida, T.Hirano, R.Ishitani, H.Siomi, M.C.Siomi, O.Nureki.
 
  ABSTRACT  
 
PIWI-clade Argonaute proteins associate with PIWI-interacting RNAs (piRNAs) and silence transposable elements in animal gonads. Here, we report the crystal structure of a silkworm PIWI-clade Argonaute, Siwi, bound to the endogenous piRNA, at 2.4 Å resolution. Siwi adopts a bilobed architecture consisting of N-PAZ and MID-PIWI lobes, in which the 5' and 3' ends of the bound piRNA are anchored by the MID-PIWI and PAZ domains, respectively. A structural comparison of Siwi with AGO-clade Argonautes reveals notable differences in their nucleic-acid-binding channels, likely reflecting the distinct lengths of their guide RNAs and their mechanistic differences in guide RNA loading and cleavage product release. In addition, the structure reveals that Siwi and prokaryotic, but not eukaryotic, AGO-clade Argonautes share unexpected similarities, such as metal-dependent 5'-phosphate recognition and a potential structural transition during the catalytic-tetrad formation. Overall, this study provides a critical starting point toward a mechanistic understanding of piRNA-mediated transposon silencing.
 

 

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