1SZW

Crystal structure of E. coli tRNA pseudouridine synthase TruD

Summary for 1SZW

• Entry DOI: 10.2210/pdb1szw/pdb
• Related: 1SB7 1SI7
• Descriptor: tRNA pseudouridine synthase D (2 entities in total)
• Functional Keywords: pseudouridine synthase, novel fold, rna modification, trud, structural proteomics in europe, spine, structural genomics, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 85933.56

Authors

Ericsson, U.B.,Nordlund, P.,Hallberg, B.M.,Structural Proteomics in Europe (SPINE) (deposition date: 2004-04-06, release date: 2004-04-20, Last modification date: 2024-11-06)

Primary citation

Ericsson, U.B.,Nordlund, P.,Hallberg, B.M.
X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold
Febs Lett., 565:59-64, 2004

PubMed Abstract: 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.

PubMed: 15135053
DOI: 10.1016/j.febslet.2004.03.085

Experimental method

X-RAY DIFFRACTION (2 Å)