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300d

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Image:300d.jpg

300d, resolution 3.000Å

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CAPTURING THE STRUCTURE OF A CATALYTIC RNA INTERMEDIATE: RNA HAMMERHEAD RIBOZYME, MN(II)-SOAKED

Overview

The crystal structure of an unmodified hammerhead RNA in the absence of, divalent metal ions has been solved, and it was shown that this ribozyme, can cleave itself in the crystal when divalent metal ions are added. This, biologically active RNA fold is the same as that found previously for two, modified hammerhead ribozymes. Addition of divalent cations at low pH, makes it possible to capture the uncleaved RNA in metal-bound form. A, conformational intermediate, having an additional Mg(II) bound to the, cleavage-site phosphate, was captured by freeze-trapping the RNA at an, active pH prior to cleavage. The most significant conformational changes, were limited to the active site of the ribozyme, and the changed, conformation requires only small additional movements to reach a proposed, transition-state.

About this Structure

300D is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme., Scott WG, Murray JB, Arnold JR, Stoddard BL, Klug A, Science. 1996 Dec 20;274(5295):2065-9. PMID:8953035

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