Journal
STRUCTURE
Volume 10, Issue 10, Pages 1415-1423Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(02)00855-9
Keywords
AAA ATPase; FtsH; metalloprotease; hexameric ring structure; substrate translocation
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FtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. We have determined the crystal structures of the Thermus thermophilus FtsH ATPase domain in the nucleotide-free and AMP-PNP- and ADP-bound states, in addition to the domain with the extra preceding segment. Combined with the mapping of the putative substrate binding region, these structures suggest that FtsH internally forms a hexameric ring structure, in which ATP binding could cause a conformational change to facilitate transport of substrates.
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