1m5o
From Proteopedia
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Gene: | SNRPA (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Transition State Stabilization by a Catalytic RNA
Overview
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 Structure
1M5O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:39:12 2008
