1: Structure. 2002 Aug;10(8):1073-83.

The crystal structure of the AAA domain of the ATP-dependent protease FtsH of
Escherichia coli at 1.5 A resolution.

Krzywda S, Brzozowski AM, Verma C, Karata K, Ogura T, Wilkinson AJ.

Structural Biology Laboratory, Department of Chemistry, University of York,
United Kingdom.

Eubacteria and eukaryotic cellular organelles have membrane-bound ATP-dependent
proteases, which degrade misassembled membrane protein complexes and play a vital
role in membrane quality control. The bacterial protease FtsH also degrades an
interesting subset of cytoplasmic regulatory proteins, including sigma(32), LpxC,
and lambda CII. The crystal structure of the ATPase module of FtsH has been
solved, revealing an alpha/beta nucleotide binding domain connected to a
four-helix bundle, similar to the AAA modules of proteins involved in DNA
replication and membrane fusion. A sulfate anion in the ATP binding pocket mimics
the beta-phosphate group of an adenine nucleotide. A hexamer form of FtsH has
been modeled, providing insights into possible modes of nucleotide binding and
intersubunit catalysis.

Publication Types: 
    Research Support, Non-U.S. Gov't

PMID: 12176385 [PubMed - indexed for MEDLINE]