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PROSITE documentation PDOC51713

Era-type guanine nucleotide-binding (G) domain profile





Description

The P-loop (see <PDOC00017>) guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G) domain that is responsible for binding and hydrolysis of guanine nucleotides.

Era is a small G-protein widely conserved in eubacteria and eukaryotes. It is essential for bacterial cell viability and is required for the maturation of 16S rRNA and assembly of the 30S ribosomal subunit. Era contains an N-terminal GTPase domain and a C-terminal distinct derivative of the type-II RNA-binding KH domain (see <PDOC50084>) [1,2,3,4].

The Era-type GTPase domain consists of a central six-stranded β-sheet flanked by five α-helices, in which the GTP-binding site is located (see <PDB:3IEU>). Guanine nucleotide molecules interact with highly conserved G protein regions G1-G5 [3].

The profile we developed covers the entire Era-type G domain.

Last update:

April 2014 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

G_ERA, PS51713; Era-type guanine nucleotide-binding (G) domain profile  (MATRIX)


References

1AuthorsLeipe D.D. Wolf Y.I. Koonin E.V. Aravind L.
TitleClassification and evolution of P-loop GTPases and related ATPases.
SourceJ. Mol. Biol. 317:41-72(2002).
PubMed ID11916378
DOI10.1006/jmbi.2001.5378

2AuthorsSullivan S.M. Mishra R. Neubig R.R. Maddock J.R.
TitleAnalysis of guanine nucleotide binding and exchange kinetics of the Escherichia coli GTPase Era.
SourceJ. Bacteriol. 182:3460-3466(2000).
PubMed ID10852878

3AuthorsTu C. Zhou X. Tropea J.E. Austin B.P. Waugh D.S. Court D.L. Ji X.
TitleStructure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis.
SourceProc. Natl. Acad. Sci. U.S.A. 106:14843-14848(2009).
PubMed ID19706445
DOI10.1073/pnas.0904032106

4AuthorsTu C. Zhou X. Tarasov S.G. Tropea J.E. Austin B.P. Waugh D.S. Court D.L. Ji X.
TitleThe Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45 near the 3' end of 16S rRNA.
SourceProc. Natl. Acad. Sci. U.S.A. 108:10156-10161(2011).
PubMed ID21646538
DOI10.1073/pnas.1017679108



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