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Structural frameworks for considering microbial protein‐ and nucleic acid‐dependent motor ATPases
Author(s) -
Thomsen Nathan D.,
Berger James M.
Publication year - 2008
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06364.x
Subject(s) - nucleic acid , biology , archaea , biochemistry , atpase , atp hydrolysis , nucleotide , motor protein , enzyme , molecular motor , microbiology and biotechnology , gene , microtubule
Summary Many fundamental cellular processes depend on enzymes that utilize chemical energy to catalyse unfavourable reactions. Certain classes of ATPases provide a particularly vivid example of the process of energy conversion, employing cycles of nucleotide turnover to move and/or rearrange biological polymers such as proteins and nucleic acids. Four well‐characterized classes of ATP‐dependent protein/nucleic acid translocases and remodelling factors are found in all three domains of life (bacteria, archaea and eukarya): additional strand catalytic ‘E' (ASCE) P‐loop NTPases, GHL proteins, actin‐fold enzymes and chaperonins. These unrelated protein superfamilies have each evolved the ability to couple ATP binding and hydrolysis to the generation of motion and force along or within their substrates. The past several years have witnessed the emergence of a wealth of structural data that help explain how such molecular engines link nucleotide turnover to conformational change. In this review, we highlight several recent advances to illustrate some of the mechanisms by which each family of ATP‐dependent motors facilitates the rearrangement and movement of proteins, protein complexes and nucleic acids.