2goz
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(New page: 200px<br /><applet load="2goz" size="350" color="white" frame="true" align="right" spinBox="true" caption="2goz, resolution 2.20Å" /> '''The 2.2 A structure ...)
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Revision as of 18:04, 29 January 2008
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The 2.2 A structure of a full-length catalytically active hammerhead ribozyme
Overview
Minimal hammerhead ribozymes have been characterized extensively by static, and time-resolved crystallography as well as numerous biochemical, analyses, leading to mutually contradictory mechanistic explanations for, catalysis. We present the 2.2 A resolution crystal structure of a, full-length Schistosoma mansoni hammerhead ribozyme that permits us to, explain the structural basis for its 1000-fold catalytic enhancement. The, full-length hammerhead structure reveals how tertiary interactions, occurring remotely from the active site prime this ribozyme for catalysis., G-12 and G-8 are positioned consistent with their previously suggested, roles in acid-base catalysis, the nucleophile is aligned with a scissile, phosphate positioned proximal to the A-9 phosphate, and previously, unexplained roles of other conserved nucleotides become apparent within, the context of a distinctly new fold that nonetheless accommodates the, previous structural studies. These interactions permit us to explain the, previously irreconcilable sets of experimental results in a unified, consistent, and unambiguous manner.
About this Structure
2GOZ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Tertiary contacts distant from the active site prime a ribozyme for catalysis., Martick M, Scott WG, Cell. 2006 Jul 28;126(2):309-20. Epub 2006 Jul 20. PMID:16859740
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