Corpus ID: 40382244

Sequence and Structure of Clp P , the Proteolytic Component of the ATP-dependent Clp Protease of Escherichia COG *

@inproceedings{Maurizi2001SequenceAS,
  title={Sequence and Structure of Clp P , the Proteolytic Component of the ATP-dependent Clp Protease of Escherichia COG *},
  author={M. Maurizi and W. P. Clark and Yoko Katayama and Stuart RudikoffJI and J. Pumphrey and B. Bowers and Susan GottesmanS},
  year={2001}
}
  • M. Maurizi, W. P. Clark, +4 authors Susan GottesmanS
  • Published 2001
  • The ATP-dependent Clp protease of Escherichia coli contains two dissimilar components: the Clp A regulatory polypeptide, with two ATP binding sites and intrinsic ATPase activity, and the Clp P subunit, which contains the proteolytic active site. The DNA sequence of the clpP gene predicts a protein of 207 amino acids (Mr 21,679), which is in close agreement with the size determined by sodium dodecyl sulfate-gel electrophoresis of purified Clp P. Clp P has a native M, of -240,000, and electron… CONTINUE READING
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