Structural Basis for Glucan Phosphatase Function in Photosynthetic Organisms

有了这个奖项，化学部的生命过程化学计划正在资助肯塔基州大学的克雷格范德库伊博士研究碳水化合物代谢的一个基本的，但还不太了解的方面。 植物以淀粉中的碳水化合物的形式储存能量。淀粉非常适合储存能量，但使其能够储存能量的特性对释放能量构成了障碍。植物利用淀粉成分的直接化学修饰来克服这一障碍，从而实现有效和快速的能量释放。虽然具有明显的生物重要性，但我们对这是如何发生的理解存在关键差距。在这项研究中，结构生物学和生物化学的工具来解决这些关键问题。理解和控制这种修饰具有相当大的希望，作为一种创新策略，既可以理解生命系统中这一过程的化学过程，又可以利用它来设计和利用淀粉。该项目影响学生在基础研究和应用研究方面的培训。创新的方法可以准备下一代的高技能的年轻科学家与尖端的跨学科研究的培训。葡聚糖磷酸酶家族成员的特异性和功能耦合的结构基础的定义，阐明这种修饰的关键功能。本研究计画利用高解析度的X光晶体学研究，结合生物化学方法，来定义葡聚糖磷酸酶的分子酶学。作为研究的一部分，确定的晶体结构将在蛋白质数据库（pdb.org）中公开。来自不同光合生物界的葡聚糖磷酸酶的结构/功能研究确定了淀粉代谢关键酶活性的共同和特定特征。这项研究的信息定义了不同光合生物中葡聚糖磷酸酶的结构机制，并探索了利用这种独特的化学碳水化合物修饰的方法。该奖项反映了NSF的法定使命，并被认为值得通过使用基金会的知识价值和更广泛的影响审查标准进行评估来支持。

With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Craig Vander Kooi from the University of Kentucky to investigate a fundamental and as yet poorly understood aspect of carbohydrate metabolism. Plants store energy in the form of carbohydrates in starch. Starch is ideally suited to store energy, but the properties that make it able to store the energy present a barrier to releasing the energy. Plants utilize direct chemical modification of the components of starch to overcome this barrier, allowing efficient and rapid energy release. While of clear biological importance, there are key gaps in our understanding of how this takes place. The tools of structural biology and biochemistry are employed in this research to address these key questions. Understanding and controlling this modification has considerable promise as an innovative strategy to both understand the chemistry of this process in living systems and harness it to engineer and utilize starch. This project impacts training of students in both fundamental and applied research. Innovative approaches allow preparation of the next generation of highly skilled young scientists with training in cutting edge interdisciplinary research.The structural basis for the specificity and functional coupling of the members of glucan phosphatase family members are defined, elucidating the critical function of this modification. This research project utilizes high resolution X-ray crystallographic studies coupled to biochemical methodology to define the molecular enzymology of glucan phosphatases. Crystal structures determined as part of the studies will be made publicly available in the Protein DataBank (pdb.org). Structure/function studies of glucan phosphatases from diverse kingdoms of photosynthetic organisms define the shared and specific features of enzymatic activity critical for starch metabolism. Information from this study defines the structural mechanism of glucan phosphatases in diverse photosynthetic organisms and explores methods to harness this unique chemical carbohydrate modification.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.