The Crystal Structure of the AAA Domain of the ATP-dependent Protease FtsH of Escherichia Coli at 1.5 A Resolution

Structure. 2002 Aug;10(8):1073-83. doi: 10.1016/s0969-2126(02)00806-7.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Dependent Proteases
  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • Dimerization
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins
  • Membrane Proteins / chemistry*
  • Metalloendopeptidases / chemistry*
  • Models, Biological
  • Models, Molecular
  • Molecular Structure
  • Protein Conformation*
  • Protein Folding
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Protein Subunits
  • Adenosine Triphosphate
  • ATP-Dependent Proteases
  • FtsH protein, E coli
  • Metalloendopeptidases
  • Adenosine Triphosphatases

Associated data

  • PDB/1LV7