1DJ0
THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION
Summary for 1DJ0
| Entry DOI | 10.2210/pdb1dj0/pdb |
| Descriptor | PSEUDOURIDINE SYNTHASE I, CHLORIDE ION (3 entities in total) |
| Functional Keywords | alpha/beta fold, rna-binding motif, rna-modifying enzyme, lyase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 59518.64 |
| Authors | Foster, P.G.,Huang, L.,Santi, D.V.,Stroud, R.M. (deposition date: 1999-11-30, release date: 2000-05-31, Last modification date: 2024-02-07) |
| Primary citation | Foster, P.G.,Huang, L.,Santi, D.V.,Stroud, R.M. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nat.Struct.Biol., 7:23-27, 2000 Cited by PubMed Abstract: 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. PubMed: 10625422DOI: 10.1038/71219 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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