SNAP annotations: PDB entry 1zzn

PDB-id

1zzn; DSSR-derived features in text and JSON formats; DNAproDB

Class

structural protein-RNA

Method

X-ray (3.37 Å)

Summary

Crystal structure of a group i intron-two exon complex that includes all catalytic metal ion ligands.

Reference

Stahley MR, Strobel SA (2005): "Structural evidence for a two-metal-ion mechanism of group I intron splicing." Science, 309, 1587-1590. doi: 10.1126/science.1114994.

Abstract

We report the 3.4 angstrom crystal structure of a catalytically active group I intron splicing intermediate containing the complete intron, both exons, the scissile phosphate, and all of the functional groups implicated in catalytic metal ion coordination, including the 2'-OH of the terminal guanosine. This structure suggests that, like protein phosphoryltransferases, an RNA phosphoryltransferase can use a two-metal-ion mechanism. Two Mg2+ ions are positioned 3.9 angstroms apart and are directly coordinated by all six of the biochemically predicted ligands. The evolutionary convergence of RNA and protein active sites on the same inorganic architecture highlights the intrinsic chemical capacity of the two-metal-ion catalytic mechanism for phosphoryl transfer.