Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis

FEBS Letters

Volumn 526, Issue 1-3, 2002, Pages 66-70

  Vasilyeva, Oxana V ^a   Kolygo, Kristina B ^a   Leonova, Yulia F ^a   Potapenko, Natalia A ^a   Ovchinnikova, Tatyana V ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

ATP dependent protease; Autolysis; Escherichia coli; Functional domain; Limited proteolysis; Protease Lon

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATASE; ENDOPEPTIDASE LA; GUANINE NUCLEOTIDE; PROTEINASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; AUTOLYSIS; BACTERIAL STRAIN; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; ESCHERICHIA COLI; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; STRUCTURE ACTIVITY RELATION; WILD TYPE;

ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ATP-DEPENDENT PROTEASES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GUANOSINE DIPHOSPHATE; GUANYLYL IMIDODIPHOSPHATE; HEAT-SHOCK PROTEINS; KINETICS; PEPTIDE MAPPING; PROTEASE LA; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES;

ESCHERICHIA COLI; HOMO;

EID: 0037189926     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(02)03117-4     Document Type: Article

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