Protein phosphoglycerate

Figure 6 Apparent elastic incoherent structure factor A q(Q) for ( ) denatured and ( ) native phosphoglycerate kinase. The solid line represents the fit of a theoretical model in which a fraction of the hydrogens of the protein execute only vihrational motion (this fraction is given by the dotted line) and the rest undergo diffusion in a sphere. For more details see Ref. 25.

FIGURE 6.28 Examples of protein domains with different numbers of layers of backbone strnctnre. (a) Cytochrome c with two layers of a-helix. (b) Domain 2 of phosphoglycerate kinase, composed of a /3-sheet layer between two layers of helix, three layers overall, (c) An nnnsnal five-layer strnctnre, domain 2 of glycogen phosphorylase, a /S-sheet layer sandwiched between four layers of a-helix. (d) The concentric layers of /S-sheet (inside) and a-helix (outside) in triose phosphate isomerase. Hydrophobic residnes are bnried between these concentric layers in the same manner as in the planar layers of the other proteins. The hydrophobic layers are shaded yellow. (Jane Richarelson)... 

T21. Tougard, P., Le, T. H., Minard, P Desmadril, M., Yon, J. M., Bizebard, T., Lebras, G and Dumas, C., Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsaia. Protein Eng. 9, 181-187... 

PGM phosphoglycerate mutase RPTR receptor protein tyrosine kinase... 

Fig. 71. Examples of protein domains with different numbers of layers of backbone structure (a) two-layer cytochrome c (b) three-layer phosphoglycerate kinase domain 2 (c) four-layer triosephosphate isomerase. The arrows above each drawing point to the backbone layers.

Arabinose-binding protein domains 1 and 2 Dihydrofolate reductase Adenylate kinase Rhodanese domains 1 and 2 Glutathione reductase domains 1 and 2 Phosphoglycerate mutase Phosphoglycerate kinase domain 2 Pyruvate kinase domain 3 Hexokinase domains 1 and 2 Catalase domain 3 Aspartate aminotransferase... 

FIGURE 10.6 Protein enzyme phosphoglycerate kinase involved in the formation of adenosine-5 -triphosphate (ATP) from adenosine-5 -diphosphate (ADP). 

Phosphoglycerate kinase has been studied in both the crystal49 and solution states.50 When ATP binds to the enzyme in the crystal, little conformational change was observed. However, the protein was crystallized from sulfate, and the binding of ATP can perhaps be represented as... 

Sherman, M.A. Chen, Y. Mas, M.T. An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure. Protein Sci., 6, 882-891 (1997)... 

Kinases Direct transfer of terminal phosphoryl group of ATP to substrate Creatine kinase Adenylate kinase Hexokinasc Phosphoglycerate kinase Pyruvate kinase Protein kinase Myokinase Phosphofructokinase Type 1 (M-S-E) Type 1 Type 1 Type 1 Type 2 (S-M-E)... 

Phosphoglycerate kinase is a protein composed of two structural domains of approximately equal molecular weight (N-terminal do-mainMr 20,814 C-terminal domain Afr 23,735). The crystallographic structure has been determined (Watson et al., 1982) and can be used to calculate the hydrophobic surface exposed to water on total or partial unfolding as well as the number of hydrogen bonds and other bonds involved in the stabilization of the folded conformation. 

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