guanosine-diphosphate and phosphohistidine

guanosine-diphosphate has been researched along with phosphohistidine* in 2 studies

Other Studies

2 other study(ies) available for guanosine-diphosphate and phosphohistidine

Article	Year
Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase. Acta crystallographica. Section D, Structural biology, 2021, Mar-01, Volume: 77, Issue:Pt 3 Succinyl-CoA synthetase (SCS) catalyzes a reversible reaction that is the only substrate-level phosphorylation in the citric acid cycle. One of the essential steps for the transfer of the phosphoryl group involves the movement of the phosphohistidine loop between active site I, where CoA, succinate and phosphate bind, and active site II, where the nucleotide binds. Here, the first crystal structure of SCS revealing the conformation of the phosphohistidine loop in site II of the porcine GTP-specific enzyme is presented. The phosphoryl transfer bridges a distance of 29 Å between the binding sites for phosphohistidine in site I and site II, so these crystal structures support the proposed mechanism of catalysis by SCS. In addition, a second succinate-binding site was discovered at the interface between the α- and β-subunits of SCS, and another magnesium ion was found that interacts with the side chains of Glu141β and Glu204β via water-mediated interactions. These glutamate residues interact with the active-site histidine residue when it is bound in site II. Topics: Animals; Binding Sites; Biocatalysis; Crystallization; Crystallography, X-Ray; Glutamic Acid; Guanosine Diphosphate; Guanosine Triphosphate; Histidine; Magnesium; Models, Molecular; Protein Conformation; Succinate-CoA Ligases; Succinic Acid; Swine	2021
ras proteins enhance the phosphorylation of a 38 kDa protein (p38) in rat liver plasma membrane. FEBS letters, 1987, Jun-08, Volume: 217, Issue:1 Phosphorylation of a 38 kDa protein (p38) present in rat liver plasma membrane has been shown for the first time to be enhanced by ras proteins. This increase in phosphorylation is about 3-16-fold depending on the incubation time and the type of ras protein used. Acid treatment removes phosphate from this protein suggesting that the phosphorylation involves phosphoramidate derivatives of basic amino acids. Experiments carried out in the presence of diethylpyrocarbonate suggest that the phosphorylation occurs on (a) histidine residue(s). It is probable that the function of p38 in the cell is modulated by ras proteins through phosphorylation. The significance of phosphorylation of p38 in terms of malignant transformation is presently known. Topics: Animals; Diethyl Pyrocarbonate; Guanosine Diphosphate; Histidine; Liver; Male; Membrane Proteins; Oncogene Protein p21(ras); Oncogene Proteins, Viral; Phosphorylation; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins p21(ras); Rats; Rats, Inbred Strains	1987

Article

Year

Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase.

Acta crystallographica. Section D, Structural biology, 2021, Mar-01, Volume: 77, Issue:Pt 3

Succinyl-CoA synthetase (SCS) catalyzes a reversible reaction that is the only substrate-level phosphorylation in the citric acid cycle. One of the essential steps for the transfer of the phosphoryl group involves the movement of the phosphohistidine loop between active site I, where CoA, succinate and phosphate bind, and active site II, where the nucleotide binds. Here, the first crystal structure of SCS revealing the conformation of the phosphohistidine loop in site II of the porcine GTP-specific enzyme is presented. The phosphoryl transfer bridges a distance of 29 Å between the binding sites for phosphohistidine in site I and site II, so these crystal structures support the proposed mechanism of catalysis by SCS. In addition, a second succinate-binding site was discovered at the interface between the α- and β-subunits of SCS, and another magnesium ion was found that interacts with the side chains of Glu141β and Glu204β via water-mediated interactions. These glutamate residues interact with the active-site histidine residue when it is bound in site II.

Topics: Animals; Binding Sites; Biocatalysis; Crystallization; Crystallography, X-Ray; Glutamic Acid; Guanosine Diphosphate; Guanosine Triphosphate; Histidine; Magnesium; Models, Molecular; Protein Conformation; Succinate-CoA Ligases; Succinic Acid; Swine

2021

ras proteins enhance the phosphorylation of a 38 kDa protein (p38) in rat liver plasma membrane.

FEBS letters, 1987, Jun-08, Volume: 217, Issue:1

Phosphorylation of a 38 kDa protein (p38) present in rat liver plasma membrane has been shown for the first time to be enhanced by ras proteins. This increase in phosphorylation is about 3-16-fold depending on the incubation time and the type of ras protein used. Acid treatment removes phosphate from this protein suggesting that the phosphorylation involves phosphoramidate derivatives of basic amino acids. Experiments carried out in the presence of diethylpyrocarbonate suggest that the phosphorylation occurs on (a) histidine residue(s). It is probable that the function of p38 in the cell is modulated by ras proteins through phosphorylation. The significance of phosphorylation of p38 in terms of malignant transformation is presently known.

Topics: Animals; Diethyl Pyrocarbonate; Guanosine Diphosphate; Histidine; Liver; Male; Membrane Proteins; Oncogene Protein p21(ras); Oncogene Proteins, Viral; Phosphorylation; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins p21(ras); Rats; Rats, Inbred Strains

1987