Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent

Journal of Biological Chemistry

Volumn 283, Issue 48, 2008, Pages 33258-33266

  Park, Eunyong ^a   Jung, Wook Lee ^a   Soo, Hyun Eom ^b   Jae, Hong Seol ^a   Chin, Ha Chung ^a  

^a Seoul National University   (South Korea)

^b Gwangju Institute of Science and Technology (GIST)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

FLOW INTERACTIONS; FUNCTIONS; NUCLEIC ACIDS; PROBABILITY DENSITY FUNCTION;

ACTIVE SITES; ALLOSTERIC MECHANISMS; ATP BINDINGS; ATP HYDROLYSES; CATALYTIC FUNCTIONS; DELETION MUTANTS; DODECAMER; HEXAMER; MOLECULAR MECHANISMS; ORDERS OF MAGNITUDES; PROTEASOME INHIBITORS; RECIPROCAL CONTROLS;

BINDING SITES;

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; HSLU ENZYME; HSLV ENZYME; NUCLEOTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SUBSTRATE; ENZYME SUBUNIT; GENE DELETION; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN PROTEIN INTERACTION;

ADENOSINE TRIPHOSPHATASES; ALLOSTERIC REGULATION; CATALYTIC DOMAIN; CYSTEINE PROTEINASE INHIBITORS; ENDOPEPTIDASE CLP; ENZYME ACTIVATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; LEUPEPTINS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SEQUENCE DELETION;

EID: 57749083505     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M805411200     Document Type: Article

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