<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Torelli AT</submitter><funding>NCRR NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>1052-70</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1894929</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(7)</volume><pubmed_abstract>The potential for water to participate in RNA catalyzed reactions has been the topic of several recent studies. Here, we report crystals of a minimal, hinged hairpin ribozyme in complex with the transition-state analog vanadate at 2.05 A resolution. Waters are present in the active site and are discussed in light of existing views of catalytic strategies employed by the hairpin ribozyme. A second structure harboring a 2',5'-phosphodiester linkage at the site of cleavage was also solved at 2.35 A resolution and corroborates the assignment of active site waters in the structure containing vanadate. A comparison of the two structures reveals that the 2',5' structure adopts a conformation that resembles the reaction intermediate in terms of (1) the positioning of its nonbridging oxygens and (2</pubmed_abstract><journal>RNA (New York, N.Y.)</journal><pubmed_title>A comparison of vanadate to a 2'-5' linkage at the active site of a small ribozyme suggests a role for water in transition-state stabilization.</pubmed_title><pmcid>PMC1894929</pmcid><funding_grant_id>R01 GM063162</funding_grant_id><funding_grant_id>R01 GM063162-05</funding_grant_id><funding_grant_id>R01 GM63162</funding_grant_id><funding_grant_id>P41 RR001209</funding_grant_id><funding_grant_id>P41 RR001209-298120</funding_grant_id><pubmed_authors>Krucinska J</pubmed_authors><pubmed_authors>Wedekind JE</pubmed_authors><pubmed_authors>Torelli AT</pubmed_authors></additional><is_claimable>false</is_claimable><name>A comparison of vanadate to a 2'-5' linkage at the active site of a small ribozyme suggests a role for water in transition-state stabilization.</name><description>The potential for water to participate in RNA catalyzed reactions has been the topic of several recent studies. Here, we report crystals of a minimal, hinged hairpin ribozyme in complex with the transition-state analog vanadate at 2.05 A resolution. Waters are present in the active site and are discussed in light of existing views of catalytic strategies employed by the hairpin ribozyme. A second structure harboring a 2',5'-phosphodiester linkage at the site of cleavage was also solved at 2.35 A resolution and corroborates the assignment of active site waters in the structure containing vanadate. A comparison of the two structures reveals that the 2',5' structure adopts a conformation that resembles the reaction intermediate in terms of (1) the positioning of its nonbridging oxygens and (2</description><dates><release>2007-01-01T00:00:00Z</release><publication>2007 Jul</publication><modification>2025-04-04T10:35:23.468Z</modification><creation>2019-03-27T02:04:09Z</creation></dates><accession>S-EPMC1894929</accession><cross_references><pubmed>17488874</pubmed><doi>10.1261/rna.510807</doi></cross_references></HashMap>