Structure/Function Analysis of Protein-Protein Interactions and Role of Dynamic Motions in Mercuric Ion Reductase.

Miller, S. M.

Technical Information Center Oak Ridge Tennessee

关键词: Proteins;    Mercury(Metal);    Functions;    Enzymes;    Detoxification;   

RP-ID  :  DE2005840156

学科分类：工程和技术（综合）

美国|英语

来源: National Technical Reports Library

【 摘 要 】

This report summarizes the activities and findings of our structure/function studies of the bacterial detoxification enzyme mercuric ion reductase. The objectives of the work were to obtain crystal structure information for the catalytic core of this enzyme, use the information to investigate the importance of specific parts of the enzyme to its function, and investigate the role of one domain of the enzyme in its function within cells. We describe the accomplishments towards these goals including many structures of the wild type and mutant forms of the enzyme that highlight its interactions with its Hg(II) substrate, elucidation of the role of the N-terminal domain in vitro and in vivo, and elucidation of the roles of at two conserved residues in the core in the mechanism of catalysis.