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1m5p
From Proteopedia
| 1m5p, resolution 2.60Å () | |||||||||
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| Ligands: | |||||||||
| Non-Standard Residues: | |||||||||
| Gene: | SNRPA (Homo sapiens) | ||||||||
| Related: | 1m5k, 1m5o, 1m5v | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Transition State Stabilization by a Catalytic RNA
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1m5p is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Rupert PB, Massey AP, Sigurdsson ST, Ferre-D'Amare AR. Transition state stabilization by a catalytic RNA. Science. 2002 Nov 15;298(5597):1421-4. Epub 2002 Oct 10. PMID:12376595 doi:10.1126/science.1076093
