|PROSITE documentation PDOC51706 [for PROSITE entry PS51706]|
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.
Within the translation factor-related (TRAFAC) class of P-loop GTPases, the EngB-type is widespread, but not ubiquitous in all three superkingdoms (missing, for example, from the Crenarchaeota, Caenorhabditis, and Drosophila). Proteins of the EngB-type GTPase family are involved in the biogenesis of ribosomes and are essential for the survival of a wide range of bacteria [1,2,3].
The EngB-type GTPase is comprised of a central β-sheet flanked by α-helices (see <PDB:1SUL>), in which semi-conserved residues involved in nucleotide binding are located in five motifs, called G1-G5. The G1 region (GxxxxGKS) forms the P-loop that is responsible for binding the phosphate groups of the guanine nucleotide. The G2 region corresponds to the switch I loop, which contains the consensus motif PGxT. The invariant threonine residue is responsible for binding a magnesium ion required for catalysis. The G3 region corresponds to the Walker B motif (DxxG), which forms part of switch II. The G4 (TKxD) and G5 motifs are involved in interactions with the guanine moiety of the substrate [2,3].
The profile we developed covers the entire EngB-type G domain.Last update:
February 2014 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Leipe D.D. Wolf Y.I. Koonin E.V. Aravind L.|
|Title||Classification and evolution of P-loop GTPases and related ATPases.|
|Source||J. Mol. Biol. 317:41-72(2002).|
|2||Authors||Ruzheinikov S.N. Das S.K. Sedelnikova S.E. Baker P.J. Artymiuk P.J. Garcia-Lara J. Foster S.J. Rice D.W.|
|Title||Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis.|
|Source||J. Mol. Biol. 339:265-278(2004).|
|3||Authors||Chan K.-H. Wong K.-B.|
|Title||Structure of an essential GTPase, YsxC, from Thermotoga maritima.|
|Source||Acta Crystallogr. F 67:640-646(2011).|