crystal structure of cryptosporidium parvum pyruvate kinase隐孢子虫的晶体结构以及丙酮酸激酶.pdfVIP

Crystal Structure of Cryptosporidium parvum Pyruvate Kinase 1 1 3 2,4 William J. Cook , Olga Senkovich , Khadijah Aleem , Debasish Chattopadhyay * 1 Department of Pathology, University of Alabama at Birmingham, Birmingham, Alabama, United States of America, 2 Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama, United States of America, 3 Ronald E. McNair Scholar Program, University of Alabama at Birmingham, Birmingham, Alabama, United States of America, 4 Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama, United States of America Abstract Pyruvate kinase plays a critical role in cellular metabolism of glucose by serving as a major regulator of glycolysis. This tetrameric enzyme is allosterically regulated by different effector molecules, mainly phosphosugars. In response to binding of effector molecules and substrates, significant structural changes have been identified in various pyruvate kinase structures. Pyruvate kinase of Cryptosporidium parvum is exceptional among known enzymes of protozoan origin in that it exhibits no allosteric property in the presence of commonly known effector molecules. The crystal structure of pyruvate ˚ kinase from C. parvum has been solved by molecular replacement techniques and refined to 2.5 A resolution. In the active site a glycerol molecule is located near the c-phosphate site of ATP, and the protein structure displays a partially closed active site. However, unlike other structures where the active site is