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
Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine in structural RNA. The pseudouridine synthase TruD, that modifies U13 in tRNA, belongs to a recently identified and large family of pseudouridine synthases present in all kingdoms of life. We report here the crystal structure of Escherichia coli TruD at 2.0 A resolution. The structure reveals an overall V-shaped molecule with an RNA-binding cleft formed between two domains: a catalytic domain and an insertion domain. The catalytic domain has a fold similar to that of the catalytic domains of previously characterised pseudouridine synthases, whereas the insertion domain displays a novel fold.
X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold.,Ericsson UB, Nordlund P, Hallberg BM FEBS Lett. 2004 May 7;565(1-3):59-64. PMID:15135053[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
- ↑ Ericsson UB, Nordlund P, Hallberg BM. X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold. FEBS Lett. 2004 May 7;565(1-3):59-64. PMID:15135053 doi:10.1016/j.febslet.2004.03.085