1m5p: Difference between revisions

Revision as of 23:16, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1m5p.png

Template:STRUCTURE 1m5p

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

Template:ABSTRACT PUBMED 12376595

About this StructureAbout this Structure

1M5P 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

Page seeded by OCA on Wed Jul 2 23:16:01 2008

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OCA

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-[[Image:1m5p.gif|left|200px]]
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 {{STRUCTURE_1m5p|  PDB=1m5p  |  SCENE=  }}
-'''Transition State Stabilization by a Catalytic RNA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12376595}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12376595}}
 ==About this Structure==
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 [[Category: Hairpin ribozyme]]
 [[Category: U1a rna binding protein]]
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