Download MendeleyThe crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution.
Krzywda, S., Brzozowski, A.M., Verma, C., Karata, K., Ogura, T., Wilkinson, A.J.(2002) Structure 10: 1073-1083
- PubMed: 12176385
- DOI: https://doi.org/10.1016/s0969-2126(02)00806-7
- Primary Citation of Related Structures:
1LV7 - PubMed Abstract:
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.
Organizational Affiliation:
Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom.
