PROSITE documentation PDOC51715GB1/RHD3-type guanine nucleotide-binding (G) domain profile
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.
The GB1/RHD3 GTPase family contains a large G domain (~230 amino acids). It is widespread in eukaryotes, but not detectable in bacteria or archaea. One conserved subfamily is typified by the Arabidopsis protein root hair defective 3 (RHD3), whose othologs are present in all crown group eukaryotes. The other subfamily is typified by the interferon γ-induced antiviral GB1 protein that is conserved in animals. The other GTPases of this subfamily are the brain finger proteins (BFPs), in which the GTPase domain is combined with an N-terminal RING finger domain (see <PDOC00449>), which implicates these proteins in ubiquitin-mediated signaling. Most members of this family have a large C-terminal, α-helical extension that probably participates in protein-protein interactions. The GB1/RHD3-type G domain has a low intrinsic affinity for nucleotide and often depends on nucleotide-dependent homodimerization to facilitate GTP hydrolysis [1,2,3,4,5,6].
The large GB1/RHD3-type G domain consists of a six-stranded β-sheet surrounded by eight helices (see <PDB:1DG3>). It contains the conserved sequence elements of GTP-binding proteins with modifications [2,4,6].
The profile we developed covers the entire GB1/RHD3-type G domain.
Last update:April 2014 / First entry.
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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). | |
| PubMed ID | 11916378 | |
| DOI | 10.1006/jmbi.2001.5378 |
| 2 | Authors | Prakash B. Praefcke G.J.K. Renault L. Wittinghofer A. Herrmann C. |
| Title | Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. | |
| Source | Nature 403:567-571(2000). | |
| PubMed ID | 10676968 | |
| DOI | 10.1038/35000617 |
| 3 | Authors | Prakash B. Renault L. Praefcke G.J.K. Herrmann C. Wittinghofer A. |
| Title | Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism. | |
| Source | EMBO J. 19:4555-4564(2000). | |
| PubMed ID | 10970849 | |
| DOI | 10.1093/emboj/19.17.4555 |
| 4 | Authors | Ghosh A. Praefcke G.J.K. Renault L. Wittinghofer A. Herrmann C. |
| Title | How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. | |
| Source | Nature 440:101-104(2006). | |
| PubMed ID | 16511497 | |
| DOI | 10.1038/nature04510 |
| 5 | Authors | Stefano G. Renna L. Moss T. McNew J.A. Brandizzi F. |
| Title | In Arabidopsis, the spatial and dynamic organization of the endoplasmic reticulum and Golgi apparatus is influenced by the integrity of the C-terminal domain of RHD3, a non-essential GTPase. | |
| Source | Plant J. 69:957-966(2012). | |
| PubMed ID | 22082223 | |
| DOI | 10.1111/j.1365-313X.2011.04846.x |
| 6 | Authors | Byrnes L.J. Sondermann H. |
| Title | Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 108:2216-2221(2011). | |
| PubMed ID | 21220294 | |
| DOI | 10.1073/pnas.1012792108 |
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