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

Krzywda, S., Brzozowski, A.M, Verma, C., Karata, K., Ogura, T. and Wilkinson, A.J. (2002) The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Å resolution. Structure, 10 (8). pp. 1073-1083. ISSN 0969-2126

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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 σ32, LpxC, and λ CII. The crystal structure of the ATPase module of FtsH has been solved, revealing an α/β 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 β-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.

Item Type: Article
Institution: The University of York
Academic Units: The University of York > Chemistry (York)
Depositing User: York RAE Import
Date Deposited: 09 Feb 2009 14:18
Last Modified: 09 Feb 2009 14:18
Published Version: http://dx.doi.org/10.1016/S0969-2126(02)00806-7
Status: Published
Publisher: Elsevier
Identification Number: 10.1016/S0969-2126(02)00806-7
URI: http://eprints.whiterose.ac.uk/id/eprint/7684

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