SIR Chemistry Investigation Abstract
EXPLORATION OF THE 3-D ATOMIC STRUCTURE OF URIDYLATE KINASE IN ARCHAEOGLOBUS FULGIDUS USING THE TECHNIQUE OF X-RAY CRYSTALLOGRAPHY
Presenter:
Chaoran Chen, Illinois Mathematics and Science Academy
Advisor:
Dr. Lisa Keefe, University of Chicago
Abstract:
Archaeglobus fulgidus is an anaerobe that may be used in gathering and detoxifying metal; it is also known to cause corrosion in iron, steel, and gas processing systems. Uridylate kinase (UMP Kinase) is involved in the reaction ATP + UMP ? ADP + UDP, which occurs during de novo synthesis of pyrimidine nucleotides in archaeoglobes and bacteria and is essential to the survival of these organisms; however, the same reaction does not occur in humans. Therefore, this protein potentially could be used as an antimicrobial target. In this project, we sought to solve the 3-D atomic structure of UMP Kinase in Archaeoglobus fulgidus using the technique x-ray protein crystallography. The protein was brought to supersaturation using the hanging-drop method, forming thin needle crystals. After cryoprotecting the crystals, we mounted them onto the ID (insertion device) beamline, collected x-ray diffraction data, and we are attempting to solve the structure using molecular replacement. The resulting structure of UMP Kinase and its implications will be discussed.