Summary for 1SGV
| Entry DOI | 10.2210/pdb1sgv/pdb |
| Descriptor | tRNA pseudouridine synthase B (2 entities in total) |
| Functional Keywords | hinged motion, trna modification, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, lyase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 67721.72 |
| Authors | Chaudhuri, B.N.,Chan, S.,Perry, L.J.,Yeates, T.O.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2004-02-24, release date: 2004-03-02, Last modification date: 2023-08-23) |
| Primary citation | Chaudhuri, B.N.,Chan, S.,Perry, L.J.,Yeates, T.O. Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase from Mycobacterium tuberculosis: a hinge at the base of the catalytic cleft. J.Biol.Chem., 279:24585-24591, 2004 Cited by PubMed Abstract: The three-dimensional structure of the RNA-modifying enzyme, psi55 tRNA pseudouridine synthase from Mycobacterium tuberculosis, is reported. The 1.9-A resolution crystal structure reveals the enzyme, free of substrate, in two distinct conformations. The structure depicts an interesting mode of protein flexibility involving a hinged bending in the central beta-sheet of the catalytic module. Key parts of the active site cleft are also found to be disordered in the substrate-free form of the enzyme. The hinge bending appears to act as a clamp to position the substrate. Our structural data furthers the previously proposed mechanism of tRNA recognition. The present crystal structure emphasizes the significant role that protein dynamics must play in tRNA recognition, base flipping, and modification. PubMed: 15028724DOI: 10.1074/jbc.M401045200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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