1m5o: Difference between revisions

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[[Image:1m5o.gif|left|200px]]
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[[Image:1m5o.png|left|200px]]


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{{STRUCTURE_1m5o|  PDB=1m5o  |  SCENE=  }}  
{{STRUCTURE_1m5o|  PDB=1m5o  |  SCENE=  }}  


'''Transition State Stabilization by a Catalytic RNA'''
===Transition State Stabilization by a Catalytic RNA===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12376595}}


==About this Structure==
==About this Structure==
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[[Category: U1a rna binding protein]]
[[Category: U1a rna binding protein]]
[[Category: Vandate]]
[[Category: Vandate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:39:56 2008''
 
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Revision as of 23:16, 2 July 2008

File:1m5o.png

Template:STRUCTURE 1m5o

Transition State Stabilization by a Catalytic RNATransition State Stabilization by a Catalytic RNA

Template:ABSTRACT PUBMED 12376595

About this StructureAbout this Structure

1M5O is a Single protein structure of sequence from Homo sapiens. 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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