1M5P

Transition State Stabilization by a Catalytic RNA

Summary for 1M5P

• Entry DOI: 10.2210/pdb1m5p/pdb
• Related: 1M5K 1M5O 1M5V
• Descriptor: RNA INHIBITOR SUBSTRATE, RNA HAIRPIN RIBOZYME, U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A, ... (6 entities in total)
• Functional Keywords: hairpin ribozyme, catalytic rna, u1a rna binding protein, cl5*, translation-rna complex, translation/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P09012
• Total number of polymer chains: 8
• Total formula weight: 96645.51

Authors

Rupert, P.B.,Massey, A.,Sigurdsson, S.T.,Ferre-D'Amare, A.R. (deposition date: 2002-07-09, release date: 2002-10-12, Last modification date: 2024-02-14)

Primary citation

Rupert, P.B.,Massey, A.P.,Sigurdsson, S.T.,Ferre-D'Amare, A.R.
Transition state stabilization by a catalytic RNA
Science, 298:1421-1424, 2002

PubMed Abstract: 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.

PubMed: 12376595
DOI: 10.1126/science.1076093

Experimental method

X-RAY DIFFRACTION (2.6 Å)