Structural highlights
Function
[TRUD_ECOLI] Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.[1]
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
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.
Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold.,Kaya Y, Del Campo M, Ofengand J, Malhotra A J Biol Chem. 2004 Apr 30;279(18):18107-10. Epub 2004 Mar 3. PMID:14999002[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kaya Y, Ofengand J. A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya. RNA. 2003 Jun;9(6):711-21. PMID:12756329
- ↑ 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. 2004 Apr 30;279(18):18107-10. Epub 2004 Mar 3. PMID:14999002 doi:http://dx.doi.org/10.1074/jbc.C400072200
