The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution (Q27639497)

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object named as

Szymon Krzywda

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author name string

Andrzej M Brzozowski

2

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Chandra Verma

3

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Kiyonobu Karata

4

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Teru Ogura

Structure and mechanism of ATP-dependent proteases

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publication date

August 2002

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published in

Structure

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volume

10

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issue

8

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page(s)

1073-83

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cites work

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Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA.

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Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli.

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Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli

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Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.

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Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)

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Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.

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The HflB protease of Escherichia coli degrades its inhibitor lambda cIII

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Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease

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Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism

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Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli

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Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP

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Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8

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Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

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