1SI7
Structure of E. coli tRNA psi 13 pseudouridine synthase TruD
Summary for 1SI7
| Entry DOI | 10.2210/pdb1si7/pdb |
| Descriptor | tRNA pseudouridine synthase D (2 entities in total) |
| Functional Keywords | trud, pseudouridine synthase, trna, novel fold, lyase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 41311.76 |
| Authors | Kaya, Y.,Del Campo, M.,Ofengand, J.,Malhotra, A. (deposition date: 2004-02-27, release date: 2004-03-16, Last modification date: 2024-04-03) |
| Primary citation | Kaya, Y.,Del Campo, M.,Ofengand, J.,Malhotra, A. Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold J.Biol.Chem., 279:18107-18110, 2004 Cited by PubMed Abstract: TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNA(Glu) to pseudouridine. It has little sequence homology with the other 10 pseudouridine synthases in E. coli which themselves have been grouped into four related protein families. Crystal structure determination of TruD revealed a two domain structure consisting of a catalytic domain that differs in sequence but is structurally very similar to the catalytic domain of other pseudouridine synthases and a second large domain (149 amino acids, 43% of total) with a novel alpha/beta fold that up to now has not been found in any other protein. PubMed: 14999002DOI: 10.1074/jbc.C400072200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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