PHOSPHOENOLPYRUVATE CARBOXYKINASE, FROM E COLI

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. PCK plays a critical role in gluconeogenesis. Under saturating conditions of Mg and ATP, PCK is activated 6 fold by the addition of Ca and 4 fold by Mn. Digestion of PCK by trypsin results in the cleavage of 25% of the C-terminus. Trypsin digested PCK, or truncated PCK, lost its ability to be activated by Ca; however Mn activation remained. Truncated PCK was found to reattain 2-fold activation by addition of Ca. In the hope of attaining a clear understanding of Pck activation by Ca and Mn, and how Ca activation can be regained four unique truncated Pck complexes were crystallized. It is believed knowledge of the crystal structure of truncated PCK may aid in the treatment of diabetes. Specifically it is believed a PCK inhibitor may one day reduced the need for insulin.