PF21680

tRNA modifying enzyme MnmG/GidA C-terminal helical domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameGIDA_C_1st
Author Punta M;0000-0002-0050-0676 Eberhardt R;0000-0001-6152-1369 Chuguransky S;0000-0002-0520-0736
Sequence Ontology0000417

Description

The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA
[1]
and, in particular the small bundle, to be responsible for the interaction with protein MnmE
[2]
. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, Pfam:PF12631. This entry represents the first helices of the GidA associated domain. The last three helices are covered in Pfam:PF13932.

References

1.Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon. Osawa T, Ito K, Inanaga H, Nureki O, Tomita K, Numata T. Structure 17, 713-24, (2009). View articlePMID: 19446527

2.Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. Meyer S, Scrima A, Versees W, Wittinghofer A. J. Mol. Biol. 380, 532-47, (2008). View articlePMID: 18565343

Further reading

3. Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme. Shi R, Villarroya M, Ruiz-Partida R, Li Y, Proteau A, Prado S, Moukadiri I, Benitez-Paez A, Lomas R, Wagner J, Matte A, Velazquez-Campoy A, Armengod ME, Cygler M. J Bacteriol 191, 7614-9, (2009). View articlePMID: 19801413

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