The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site

Journal of Biological Chemistry

Volumn 279, Issue 9, 2004, Pages 8140-8148

  Botos, Istvan ^a   Melnikov, Edward E ^b   Cherry, Scott ^a   Tropea, Joseph E ^a   Khalatova, Anna G ^b   Rasulova, Fatima ^c   Dauter, Zbigniew ^a   Maurizi, Michael R ^c   Rotanova, Tatyana V ^b   Wlodawer, Alexander ^a   Gustchina, Alla ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

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

^c NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELLS; CRYSTAL STRUCTURE; OLIGOMERS; POLYPEPTIDES; PROTEINS;

AXIAL CHANNELS; HOLOENZYMES;

ESCHERICHIA COLI;

CHYMOTRYPSIN; ENDOPEPTIDASE LA; HOLOENZYME; LYSINE; PEPTIDE HYDROLASE; POLYPEPTIDE; PROTEINASE; REGULATOR PROTEIN; SERINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN PROCESSING;

ATP-DEPENDENT PROTEASES; BINDING SITES; CATALYSIS; CHYMOTRYPSIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; LYSINE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEASE LA; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SERINE; SERINE ENDOPEPTIDASES;

ANIMALIA; ESCHERICHIA COLI;

EID: 10744225162     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M312243200     Document Type: Article

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