3BDL

Crystal structure of a truncated human Tudor-SN

Summary for 3BDL

• Entry DOI: 10.2210/pdb3bdl/pdb
• Related: 2O4X
• Descriptor: Staphylococcal nuclease domain-containing protein 1, CITRIC ACID (3 entities in total)
• Functional Keywords: staphylococcal nuclease ob fold, tudor domain, cytoplasm, host-virus interaction, nucleus, phosphoprotein, transcription, transcription regulation, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: Q7KZF4
• Total number of polymer chains: 1
• Total formula weight: 64781.14

Authors

Li, C.L. (deposition date: 2007-11-15, release date: 2008-08-26, Last modification date: 2024-03-13)

Primary citation

Li, C.L.,Yang, W.Z.,Chen, Y.P.,Yuan, H.S.
Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing.
Nucleic Acids Res., 36:3579-3589, 2008

PubMed Abstract: Human Tudor-SN is involved in the degradation of hyper-edited inosine-containing microRNA precursors, thus linking the pathways of RNA interference and editing. Tudor-SN contains four tandem repeats of staphylococcal nuclease-like domains (SN1-SN4) followed by a tudor and C-terminal SN domain (SN5). Here, we showed that Tudor-SN requires tandem repeats of SN domains for its RNA binding and cleavage activity. The crystal structure of a 64-kD truncated form of human Tudor-SN further shows that the four domains, SN3, SN4, tudor and SN5, assemble into a crescent-shaped structure. A concave basic surface formed jointly by SN3 and SN4 domains is likely involved in RNA binding, where citrate ions are bound at the putative RNase active sites. Additional modeling studies provide a structural basis for Tudor-SN's preference in cleaving RNA containing multiple I.U wobble-paired sequences. Collectively, these results suggest that tandem repeats of SN domains in Tudor-SN function as a clamp to capture RNA substrates.

PubMed: 18453631
DOI: 10.1093/nar/gkn236

Experimental method

X-RAY DIFFRACTION (1.9 Å)