EC Number   |
|---|
   2.4.1.345 | crystal structures of PimA in complex with GDP and GDP-Man are determined using multiplewavelength anomalous diffraction methods at 2.4 A and 2.6 A resolution respectively |
| 2.4.1.345 | crystal structures of PimA in complex with GDP and GDP-Man is determined using multiple-wavelength anomalous diffraction methods at 2.4 and 2.6 A of resolution, respectively |
| 2.4.1.345 | crystal structures of PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including beta-strand-to-alpha-helix and alpha-helix-to-beta-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane |
| 2.4.1.345 | in complex with GDP and GDP-Man, to 2.4 and 2.6 A resolution, respectively. The structure of PimA in complex with GDP-mannose shows the two-domain organization and the catalytic machinery typical of GT-B glycosyltransferases. Model wherein PimA attaches to the membrane through its N-terminal domain, and this association leads to enzyme activation |
| 2.4.1.345 | in the presence of GDP and myo-inositol, to 2.4 A resolution, orthorhombic space group P212121, one molecule per asymmetric unit |
| 2.4.1.345 | PimA undergoes significant conformational changes upon substrate binding. The binding of the donor GDP-Man triggers an important interdomain rearrangement that stabilizes the enzyme and generates the binding site for the acceptor substrate, phosphatidyl-myo-inositol. The interaction of PimA with the beta-phosphate of GDP-Man is essential for this conformational change. Binding of phosphatidyl-myo-inositol has the opposite effect, inducing the formation of a more relaxed complex with PimA. GDP-Man stabilizes and phosphatidyl-myo-inositol destabilizes PimA by a similar enthalpic amount |
| 2.4.1.345 | PimA-GDP-Manp complex |
| 2.4.1.345 | sitting-drop vapour-diffusion method. The crystals belong to space group P2(1)2(1)2(1) with unit-cell parameters a = 37.2, b = 72.4, c = 138.2 A and diffract to 2.4 A resolution |
