1lv7

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1lv7, resolution 1.50Å

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Crystal Structure of the AAA domain of FtsH

Overview

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.

About this Structure

1LV7 is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution., Krzywda S, Brzozowski AM, Verma C, Karata K, Ogura T, Wilkinson AJ, Structure. 2002 Aug;10(8):1073-83. PMID:12176385

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