Some measurements of the shape and hydrodynamic properties of yeast phosphoglycerate kinase (E.C.2.7.2.3).
Using values obtained for sedimentation and diffusion constants the relative mass of phosphoglycerate kinase was calculated to be 45 800 +/- 1700. This value is higher than was previously estimated and the difference is thought to be caused by contamination of earlier crystalline preparations. Using the coordinates from X-ray crystallography it was found possible to calculate a frictional ratio for a linear dumb-bell (1.115) which compared well with the ratio calculated from diffusion (1.114 +/- 0.033). Since the calculated ratio for a bent molecule was 1.020 the natural state of the molecule in solution is essentially linear. From the concentration dependence of sedimentation and diffusion was calculated the effective interactive radius which resembles haemoglobin in its relationship to the molecular radius.
D008970:Molecular Weight; D010735:Phosphoglycerate Kinase; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014961:X-Ray Diffraction
D010735:Phosphoglycerate Kinase