InterPro domain: IPR006169

Several proteins have recently been shown to contain the 5 structural motifs characteristicof GTP-binding proteins [ 1 ]. These include murine DRG protein; GTP1 proteinfrom Schizosaccharomyces pombe; OBG protein from Bacillus subtilis; and several others.Although the proteins contain GTP-binding motifs and are similar to each other, they donot share sequence similarity to other GTP-binding proteins, and have thus been classedas a novel group, the GTP1/OBG family. As yet, the functions of these proteins is uncertain,but they have been shown to be important in development and normal cell metabolism[ 2 , 3 ].

The N-terminal domain of GTPase Obg has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich. These regions form six left-handed collagen-like helices packed and H-bonded together.

1. DRG: a novel developmentally regulated GTP-binding protein. Biochem. Biophys. Res. Commun. 189, 363-70
2. Sequence of the Schizosaccharomyces pombe gtp1 gene and identification of a novel family of putative GTP-binding proteins. Gene 125, 191-3
3. The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein. J. Bacteriol. 171, 1362-71