2GJW

RNA Recognition and Cleavage by an Splicing Endonuclease

Summary for 2GJW

• Entry DOI: 10.2210/pdb2gjw/pdb
• Descriptor: 5'-R(*GP*CP*GP*AP*CP*CP*GP*AP*CP*CP*AP*(DU)P*AP*GP*CP*UP*GP*CP*A)-3', 5'-R(*UP*GP*CP*AP*GP*CP*GP*GP*UP*CP*AP*(A23))-3', 5'-R(*AP*GP*GP*UP*CP*GP*C)-3', ... (4 entities in total)
• Functional Keywords: bulge-helix-bulge rna-protein complex, splicing endonuclease af, hydrolase-rna complex, hydrolase/rna
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 10
• Total formula weight: 172840.46

Authors

Xue, S.,Calvin, K.,Li, H. (deposition date: 2006-03-31, release date: 2006-09-12, Last modification date: 2025-05-14)

Primary citation

Xue, S.,Calvin, K.,Li, H.
RNA Recognition and Cleavage by an Splicing Endonuclease
Science, 312:902-910, 2006

PubMed Abstract: The RNA splicing endonuclease cleaves two phosphodiester bonds within folded precursor RNAs during intron removal, producing the functional RNAs required for protein synthesis. Here we describe at a resolution of 2.85 angstroms the structure of a splicing endonuclease from Archaeglobus fulgidus bound with a bulge-helix-bulge RNA containing a noncleaved and a cleaved splice site. The endonuclease dimer cooperatively recognized a flipped-out bulge base and stabilizes sharply bent bulge backbones that are poised for an in-line RNA cleavage reaction. Cooperativity arises because an arginine pair from one catalytic domain sandwiches a nucleobase within the bulge cleaved by the other catalytic domain.

PubMed: 16690865
DOI: 10.1126/science.1126629

Experimental method

X-RAY DIFFRACTION (2.85 Å)