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Curr Opin Struct Biol. 2003 Apr;13(2):249-55.

Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures.

Author information

1
Gene Center and Institute of Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, Germany. hopfner@lmb.uni-muenchen.de

Abstract

ATP-binding cassette (ABC)-type ATPases are chemo-mechanical engines for diverse biological pathways. ABC ATPase domains act not only in ABC transporters but also in DNA mismatch, nucleotide excision and double-strand break repair enzymes, as well as in chromosome segregation. Atomic-resolution crystal structures suggest molecular mechanisms for ABC ATPases and reveal surprisingly significant mechanistic and architectural conservation. This emerging unified structural biochemistry provides general medical and biological insights into how ABC proteins function as chemo-mechanical devices. ATP binding by the signature and Q-loop motifs drives the conformations of substrate-specific domains to accomplish diverse functions in transmembrane transport and DNA repair.

PMID:
12727520
DOI:
10.1016/s0959-440x(03)00037-x
[Indexed for MEDLINE]

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