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The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site

author

Alla Gustchina

Alexander Wlodawer

1946 -

Zbigniew Dauter

published in: Journal of Biological Chemistry

date of publication: 2004-02-27

language: English

main subject: Escherichia coli

Cites articles 51

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Benedikt M. Kessler
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Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis
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Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism

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Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
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A non-canonical lon proteinase lacking the ATPase domain employs the ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus
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Article - wd:Q27642758

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