1LV7

Crystal Structure of the AAA domain of FtsH

Summary for 1LV7

• Entry DOI: 10.2210/pdb1lv7/pdb
• Descriptor: FtsH, SULFATE ION (3 entities in total)
• Functional Keywords: alpha/beta domain, four helix bundle, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0AAI3
• Total number of polymer chains: 1
• Total formula weight: 28249.40

Authors

Krzywda, S.,Brzozowski, A.M.,Verma, C.,Karata, K.,Ogura, T.,Wilkinson, A.J. (deposition date: 2002-05-26, release date: 2002-10-09, Last modification date: 2024-03-13)

Primary citation

Krzywda, S.,Brzozowski, A.M.,Verma, C.,Karata, K.,Ogura, T.,Wilkinson, A.J.
The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution.
Structure, 10:1073-1083, 2002

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.

PubMed: 12176385
DOI: 10.1016/S0969-2126(02)00806-7

Experimental method

X-RAY DIFFRACTION (1.5 Å)