Crystallization (Comment) | Organism |
---|---|
purified enzyme hydrogenated H-RAS, residues 1-166, Sitting drop vapour diffusion, 1:1 ratio of protein solution, containing 20 mM HEPES, pH 7.5, 50 mM NaCl, 5 mM MgCl2, 1 mM DTT, and reservoir solution containing 200 mM calcium acetate, 20% w/v PEG 3350, 0.1% w/v n-octyl-beta-D-glucoside. Once the crystals has stopped growing, the hydrogenated reservoir solution is replaced with an identical reservoir solution prepared with D2O. A single crystal of the small GTPase Ras is used to collect three neutron data sets at pD 8.4, 9.0 and 9.4, in crystallo titration study using neutron protein crystallography (NPC), a method that lacks radiation damage of the cyrstals. Structure analysis at resolution of 1.9-2.1 A | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required | Homo sapiens | |
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | Homo sapiens | - |
GDP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | - |
Homo sapiens | GDP + phosphate | - |
? | |
additional information | Ras binds guanine nucleotides in its guanine nucleotide-binding cleft composed of G-box elements that are conserved among all GTPase proteins | Homo sapiens | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
RAS | - |
Homo sapiens |
small GTPase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | enzyme structure-activity analysis and Ras allosteric networks, detailed overview. The allosteric networks on Ras intimately link switch I and switch II to each other and to two other functionally important regions on the opposite side of the protein. Switch I is linked to helix 5 membrane-interacting residues at the back of the molecule, where Arg161 and Arg164 make salt bridges with the interswitch loop 3 residues Asp47 and Glu49. Switch II is normally disordered and disconnected from the network. When calcium and a negatively charged ligand bind, helix 3 shifts towards helix 4, and the entire switch II becomes ordered and linked to the Ca2+-binding pocket through an extensive water-mediated network | Homo sapiens |