Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.

Abstract:

: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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Thomsen ND,Berger JM

doi

10.1111/j.1365-2958.2008.06364.x

subject

Has Abstract

pub_date

2008-09-01 00:00:00

pages

1071-90

issue

5

eissn

0950-382X

issn

1365-2958

pii

MMI6364

journal_volume

69

pub_type

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