1m5p

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Revision as of 19:01, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1m5p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5p, resolution 2.60Å" /> '''Transition State St...)
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File:1m5p.gif


1m5p, resolution 2.60Å

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Transition State Stabilization by a Catalytic RNA

OverviewOverview

The hairpin ribozyme catalyzes sequence-specific cleavage of RNA through, transesterification of the scissile phosphate. Vanadate has previously, been used as a transition state mimic of protein enzymes that catalyze the, same reaction. Comparison of the 2.2 angstrom resolution structure of a, vanadate-hairpin ribozyme complex with structures of precursor and product, complexes reveals a rigid active site that makes more hydrogen bonds to, the transition state than to the precursor or product. Because of the, paucity of RNA functional groups capable of general acid-base or, electrostatic catalysis, transition state stabilization is likely to be an, important catalytic strategy for ribozymes.

About this StructureAbout this Structure

1M5P is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Transition state stabilization by a catalytic RNA., Rupert PB, Massey AP, Sigurdsson ST, Ferre-D'Amare AR, Science. 2002 Nov 15;298(5597):1421-4. Epub 2002 Oct 10. PMID:12376595

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