The GTPase superfamily: conserved structure and molecular mechanism

@article{Bourne1991TheGS,
  title={The GTPase superfamily: conserved structure and molecular mechanism},
  author={Henry R. Bourne and David Avram Sanders and Frank McCormick},
  journal={Nature},
  year={1991},
  volume={349},
  pages={117-127}
}
GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases—crystal structures, biochemical properties, or results of molecular genetic experiments—support and generate hypotheses relating structure to function in other members of the diverse family of GTPases. 
GTP‐binding Loop
The GTP-binding loop is an evolutionarily conserved structure found in the GTPase superfamily of proteins. The GTP-binding loop enables GTPases to bind and hydrolyse GTP molecules and makes them
GTPases: a family of molecular switches and clocks.
  • H. Bourne
  • Biology, Medicine
    Philosophical transactions of the Royal Society of London. Series B, Biological sciences
  • 1995
TLDR
Analysis of the patterns of conserved amino acid side chains on surfaces of G alpha proteins reveals interfaces with other proteins in the G-protein signal linking device.
ROP GTPases Structure-Function and Signaling Pathways1[OPEN]
Interactions between receptor like kinases and guanyl nucleotide exchange factors together with identification of effector proteins reveal putative ROP GTPases signaling cascades.
Role of GTPases in ribosome assembly.
TLDR
A review of common structural, biochemical and genetic interactions of GTPases is presented and integrated with models for their function in ribosome assembly.
Structure-function relationships of the G domain, a canonical switch motif.
TLDR
The common principle is the 160-180-residue G domain with an α,β topology that is responsible for nucleotide-dependent conformational changes and drives many biological functions.
GTP-Binding Proteins: Structures, interactions and relationships
Recently available crystal structures show that some, though not all, GTP-binding proteins have a common 'G-domain' topology, variations on which confer distinct functional properties.
RUN domains: a new family of domains involved in Ras-like GTPase signaling.
RUN domains are present in several proteins that are linked particularly to the functions of GTPases in the Rap and Rab families. They could hence play an important role in multiple Ras-like GTPase
rho and rho-Related Proteins
The Rho-like proteins form a distinct subgroup of the ras superfamily of small GTPases. They act as molecular switches having an inactive, GDP-bound and an active, GTP-bound conformation and have
Roles played by Ras subfamily proteins in the cell and developmental biology of microorganisms.
TLDR
The Ras subfamily proteins are monomeric GTPases that function as molecular switches in cellular signal transduction pathways that play a role in the growth and differentiation of single celled microorganisms.
Kinesin and myosin: molecular motors with similar engines.
Structure determination of the catalytic domains of two members of the kinesin superfamily reveals that this class of molecular motor exhibits the same architecture as myosin and suggests that these
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