DIRAS2: Distinct subgroup of the Ras family, member 2 (human)
PDB Code: 2ERX
Cells respond in many ways to environmental changes including altering gene expression, physically moving locations, changes to cell-cell interactions, differentiation and even altering their life spans. This is achieved through a signalling network that consists of several signalling pathways. The network receives multiple signals, interprets the signals, amplified and then transmits the signals. One of the best characterised signalling pathways involves the ras GTPase family. The importance of this family of small GTPases to human health was first recognised through the identification of the human H-Ras, N-Ras and K-Ras genes as being oncogenic.
DIRAS2 is the first structure of the subfamily of DIRAS small GTPases. The family members are characterised by a number of alterations that would be expected to produce a constitutively active form. The most significant is the lack of a glutamine residue, the equivalent of which is highly conserved in catalytically active small GTPases and is known to be involved in the catalysis process. DIRAS family members are also likely to use a different signalling pathway from the standard Ras-Raf-1 kinase signalling pathway as a hydrophobic residue is present in place of an Asp in Ras which forms part of the Ras-Raf-1 binding site.
Crystals of DIRAS2 were grown in the presence of the GTP nucleotide as this protein was expected to be catalytically active. Surprisingly, the crystal structure clearly showed that DIRAS2 is able to catalysis the hydrolysis of GTP as both products, GDP and Pi, are present in the electron density. These products along a Ser side chain and the Thr side chain from the Switch I loop form a square planar coordination around the Mg2+ ion. Two water molecule above and below the Mg2+ ion complete the expected octahedral coordination.

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