Literature DB >> 12658998

[Catalytic dyad Ser-Lys at the active site of Escherichia coli ATP-dependent Lon-proteinase].

T V Rotanova, E E Mel'nikov, K B Tsirul'nikov.   

Abstract

Two subfamilies of Lon proteases that differ in the structure of the fragments containing the catalytically active Ser residue were revealed by the comparison of more than sixty sequences of Lon proteases from various sources. The absence of the classic catalytic triad in the active site of Lon proteases was confirmed. The catalytic site of Lon proteases was shown to be represented by the Ser-Lys dyad.

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Year:  2003        PMID： 12658998     DOI： 10.1023/a:1022290705294

Source DB:  PubMed          Journal:  Bioorg Khim        ISSN： 0132-3423


  7 in total

1.  Structure of the N-terminal fragment of Escherichia coli Lon protease.

Authors:  Mi Li; Alla Gustchina; Fatima S Rasulova; Edward E Melnikov; Michael R Maurizi; Tatyana V Rotanova; Zbigniew Dauter; Alexander Wlodawer
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2010-07-09

Review 2.  Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.

Authors:  Tatyana V Rotanova; Istvan Botos; Edward E Melnikov; Fatima Rasulova; Alla Gustchina; Michael R Maurizi; Alexander Wlodawer
Journal:  Protein Sci       Date:  2006-08       Impact factor: 6.725

Review 3.  Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.

Authors:  Ozlem Doğan Ekici; Mark Paetzel; Ross E Dalbey
Journal:  Protein Sci       Date:  2008-09-29       Impact factor: 6.725

Review 4.  Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.

Authors:  Alexander Wlodawer; Bartosz Sekula; Alla Gustchina; Tatyana V Rotanova
Journal:  J Mol Biol       Date:  2022-02-17       Impact factor: 6.151

5.  Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family.

Authors:  Peng Wang; Eunjung Shim; Benjamin Cravatt; Richard Jacobsen; Joe Schoeniger; Apollos C Kim; Mark Paetzel; Ross E Dalbey
Journal:  Biochemistry       Date:  2008-05-14       Impact factor: 3.162

6.  Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.

Authors:  Edward E Melnikov; Anna G Andrianova; Andrey D Morozkin; Anton A Stepnov; Oksana V Makhovskaya; Istvan Botos; Alla Gustchina; Alexander Wlodawer; Tatyana V Rotanova
Journal:  Acta Biochim Pol       Date:  2008-05-26       Impact factor: 2.149

7.  Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases.

Authors:  Alla Gustchina; Mi Li; Anna G Andrianova; Arsen M Kudzhaev; George T Lountos; Bartosz Sekula; Scott Cherry; Joseph E Tropea; Ivan V Smirnov; Alexander Wlodawer; Tatyana V Rotanova
Journal:  Int J Mol Sci       Date:  2022-09-28       Impact factor: 6.208
  7 in total

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