Structural highlights
1sgv is a 2 chain structure with sequence from Myctu. This structure supersedes the now removed PDB entry 1s71. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Gene: | TRUB, RV2793C, MT2862.1, MTV002.58C, MB2816C (MYCTU) |
| Activity: | Pseudouridylate synthase, with EC number 4.2.1.70 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[TRUB_MYCTU] Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase from Mycobacterium tuberculosis: a hinge at the base of the catalytic cleft.,Chaudhuri BN, Chan S, Perry LJ, Yeates TO J Biol Chem. 2004 Jun 4;279(23):24585-91. Epub 2004 Mar 17. PMID:15028724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chaudhuri BN, Chan S, Perry LJ, Yeates TO. 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. 2004 Jun 4;279(23):24585-91. Epub 2004 Mar 17. PMID:15028724 doi:10.1074/jbc.M401045200
