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5GUH

Crystal structure of silkworm PIWI-clade Argonaute Siwi bound to piRNA

Summary for 5GUH
Entry DOI10.2210/pdb5guh/pdb
DescriptorPIWI, RNA (28-MER), MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsnuclease, rnaseh, hydrolase-rna complex, hydrolase/rna
Biological sourceBombyx mori (Silk moth)
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Cellular locationCytoplasm : A8D8P8
Total number of polymer chains2
Total formula weight110558.40
Authors
Matsumoto, N.,Nishimasu, H.,Ishitani, R.,Nureki, O. (deposition date: 2016-08-29, release date: 2016-10-19, Last modification date: 2023-11-08)
Primary citationMatsumoto, N.,Nishimasu, H.,Sakakibara, K.,Nishida, K.M.,Hirano, T.,Ishitani, R.,Siomi, H.,Siomi, M.C.,Nureki, O.
Crystal Structure of Silkworm PIWI-Clade Argonaute Siwi Bound to piRNA
Cell, 167:484-497.e9, 2016
Cited by
PubMed 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.
PubMed: 27693359
DOI: 10.1016/j.cell.2016.09.002
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2024-10-30公开中

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