Summary for 3ZD5
| Entry DOI | 10.2210/pdb3zd5/pdb |
| Related | 3ZD4 3ZP8 |
| Descriptor | HAMMERHEAD RIBOZYME, ENZYME STRAND, HAMMERHEAD RIBOZYME, SUBSTRATE STRAND (3 entities in total) |
| Functional Keywords | catalytic rna, in-line attack, hammerhead rna, stem-loop interaction, uridine turn, a-form helix, rna |
| Biological source | Schistosoma mansoni More |
| Total number of polymer chains | 2 |
| Total formula weight | 20432.93 |
| Authors | Martick, M.,Scott, W.G. (deposition date: 2012-11-24, release date: 2012-12-12, Last modification date: 2024-05-08) |
| Primary citation | Martick, M.,Scott, W.G. Tertiary contacts distant from the active site prime a ribozyme for catalysis. Cell, 126:309-320, 2006 Cited by PubMed Abstract: 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. PubMed: 16859740DOI: 10.1016/j.cell.2006.06.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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