The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I
| Autor: | P G, Foster, L, Huang, D V, Santi, R M, Stroud |
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| Rok vydání: | 2000 |
| Předmět: |
Models
Molecular Aspartic Acid Binding Sites Molecular Sequence Data RNA-Binding Proteins Hydrogen Bonding Crystallography X-Ray Protein Structure Secondary Protein Structure Tertiary Substrate Specificity RNA Transfer Anticodon Escherichia coli Amino Acid Sequence Crystallization Dimerization Uridine Conserved Sequence Hydro-Lyases Pseudouridine |
| Zdroj: | Nature structural biology. 7(1) |
| ISSN: | 1072-8368 |
| Popis: | Pseudouridine synthases catalyze the isomerization of specific uridines to pseudouridine in a variety of RNAs, yet the basis for recognition of the RNA sites or how they catalyze this reaction is unknown. The crystal structure of pseudouridine synthase I from Escherichia coli, which, for example, modifies positions 38, 39 and/or 40 in tRNA, reveals a dimeric protein that contains two positively charged, RNA-binding clefts along the surface of the protein. Each cleft contains a highly conserved aspartic acid located at its center. The structural domains have a topological similarity to those of other RNA-binding proteins, though the mode of interaction with tRNA appears to be unique. The structure suggests that a dimeric enzyme is required for binding transfer RNA and subsequent pseudouridine formation. |
| Databáze: | OpenAIRE |
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