MECHANISM OF DOMAIN MOVEMENT IN PHOSPHOGLYCERATE KINASE

底物诱导的磁区移动，这导致有源的 位裂解，是3-脱氧核糖核酸催化机理的重要组成部分。 磷酸甘油酸激酶。配基诱导繁殖的目的 这种酶的构象变化。侧链的作用 在相邻α螺旋之间的界面上的相互作用，位于 在域-域接口，他们与每个域的联系将是 使用定点突变技术进行检测。3-的位置- 磷酸甘油酸结合部位也将使用这种方法来确定。 突变对突变体催化性能的影响将是 特色化的。将对突变体的结构和稳定性进行评估 使用生化和物理方法。这些研究应该有助于 更好地理解功能重要性的机制 蛋白质的构象变化。

Substrate-induced domain movement, which results in closure of the active site cleft, is an essential part of the catalytic mechanisms of 3- phosphoglycerate kinase. The aim of propagation of ligand-induced conformational changes for this enzyme. The role of the side chain interactions at the interfaces between the adjacent alpha-helices, situated at the domain-domain interface, and their contacts with each domain will be examined using site directed mutagenesis. The location of the 3- phosphoglycerate binding site will also be determined using this approach. The effect of mutations on the catalytic properties of the mutants will be characterized. The structure and stability of mutants will be evaluated using biochemical and physical methods. These studies should contribute to a better understanding of the mechanisms of functionally-important conformational changes in proteins.