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| Content Provider | PubMed Central |
|---|---|
| Author | Torelli, Andrew T. Spitale, Robert C. Krucinska, Jolanta Wedekind, Joseph E. |
| Abstract | Reaction-intermediate analogs have been used to understand how phosphoryl-transfer enzymes promote catalysis. Herein we report the first structure of a small ribozyme crystallized with a 3′-OH, 2′,5′-linkage in lieu of the normal phosphodiester substrate. The new structure shares features of the reaction coordinate exhibited in prior ribozyme structures including a vanadate complex that mimicked the oxyphosphorane transition state. As such, the structure exhibits reaction-intermediate traits that allow direct comparison of stabilizing interactions to the 3′-OH, 2′,5′-linkage contributed by the RNA enzyme and its protein counterpart, ribonuclease. Clear similarities are observed between the respective structures including hydrogen bonds to the non-bridging oxygens of the scissile-phosphate. Other commonalities include carefully poised water molecules that may alleviate charge build-up in the transition state and placement of a positive charge near the leaving group. The advantages of 2′,5′-linkages to investigate phosphoryl-transfer reactions are discussed, and argue for their expanded use in structural studies. |
| Related Links | http://dx.doi.org/10.1016/j.bbrc.2008.04.036 |
| Ending Page | 158 |
| Page Count | 5 |
| Starting Page | 154 |
| File Format | |
| ISSN | 0006291X |
| e-ISSN | 10902104 |
| Journal | Biochemical and biophysical research communications |
| Issue Number | 1 |
| Volume Number | 371 |
| Language | English |
| Publisher Date | 2008-06-01 |
| Access Restriction | Open |
| Subject Keyword | Biophysics Cell Biology Biochemistry Molecular Biology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Biochemistry Biophysics |
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