Article
Rotary and unidirectional metal shadowing of VAT: localization of the substrate-binding domain.
Journal of structural biology - 1 Nov 2000
Rockel B, Guckenberger R, Gross H, Tittmann P, Baumeister W
Abstract excerpt
AAA-ATPases have important roles in manifold cellular processes. VAT (valosine-containing protein-like ATPase of Thermoplasma acidophilum), a hexameric archaeal member of this family, has the tripartite domain structure N-D1-D2 that is characteristic of many members of this family. N, the N-terminal domain of 20.5 kDa, has been implicated in substrate binding. We have applied rotary and unidirectional shadowing...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
