4.5 Article

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

Journal

CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 13, Issue 2, Pages 249-255

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/S0959-440X(03)00037-X

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Funding

  1. NCI NIH HHS [P01 CA92584] Funding Source: Medline

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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.

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