1LV7

Crystal Structure of the AAA domain of FtsH

1LV7 の概要

• エントリーDOI: 10.2210/pdb1lv7/pdb
• 分子名称: FtsH, SULFATE ION (3 entities in total)
• 機能のキーワード: alpha/beta domain, four helix bundle, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0AAI3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28249.40

構造登録者

Krzywda, S.,Brzozowski, A.M.,Verma, C.,Karata, K.,Ogura, T.,Wilkinson, A.J. (登録日: 2002-05-26, 公開日: 2002-10-09, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)