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Summary
| Description |
English: The crystal structure of the class I ribonuclease III (Rnt1p) from Saccharomyces cerevisiae in complex with double-stranded RNA (shown in surface representation in red). The protein is a dimer; the N-terminal domains are shown in blue and orange; the dsRNA-binding domains in cyan and tan; and the ribonuclease domains in light blue and yellow.
Rendered from PDB 4OOG. Liang YH, Lavoie M, Comeau MA, Elela SA, Ji X. Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler mechanism for substrate selection. Molecular cell. 2014 May 8;54(3):431-44. DOI: 10.1016/j.molcel.2014.03.006 |
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| Source | Own work |
| Author | Opabinia regalis |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 05:45, 7 November 2016 | | 1,800 × 900 (1.1 MB) | Opabinia regalis | {{Information |Description ={{en|1=The crystal structure of the class I ribonuclease III (Rnt1p) from ''Saccharomyces cerevisiae'' in complex with double-stranded RNA (shown in surface representation in red). The protein is a dimer; the N-terminal d... |
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