1m5v
From Proteopedia
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[[Image:1m5v.gif|left|200px]] | [[Image:1m5v.gif|left|200px]] | ||
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'''Transition State Stabilization by a Catalytic RNA''' | '''Transition State Stabilization by a Catalytic RNA''' | ||
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[[Category: Rupert, P B.]] | [[Category: Rupert, P B.]] | ||
[[Category: Sigurdsson, S T.]] | [[Category: Sigurdsson, S T.]] | ||
| - | [[Category: | + | [[Category: Catalytic rna]] |
| - | [[Category: | + | [[Category: Cleaved substrate]] |
| - | [[Category: | + | [[Category: Hairpin ribozyme]] |
| - | [[Category: | + | [[Category: U1a rna binding protein 2'3'cyclic phosphate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:40:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:40, 2 May 2008
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
1M5V 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 Sat May 3 00:40:20 2008
