Reaction cycle of Thermotoga maritima copper ATPase and conformational characterization of catalytically deficient mutants

Biochemistry

Volumn 48, Issue 22, 2009, Pages 4871-4880

  Hatori, Yuta ^a   Lewis, David ^a   Toyoshima, Chikashi ^b   Inesi, Giuseppe ^a,c  

^a CALIFORNIA PACIFIC MEDICAL CENTER   (United States)

^b UNIVERSITY OF TOKYO   (Japan)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEOGLOBUS FULGIDUS; ATP-ASE ACTIVITY; ATPASES; CATALYTIC DOMAINS; CATALYTIC TURNOVER; CONFORMATIONAL ANALYSIS; CONFORMATIONAL CHANGE; COPPER BINDING; COPPER TRANSPORT; DOMAIN MOVEMENT; FUNCTIONAL CHARACTERIZATION; HETEROLOGOUS EXPRESSION; MECHANISTIC STUDIES; METAL BINDING DOMAIN; METAL BINDING SITES; METALLOENZYMES; N-TERMINAL; NUCLEOTIDE-BINDING DOMAIN; OPTIMAL POSITION; P-TYPE; PHOSPHOENZYME; PHOSPHORYL TRANSFER; PROTEOLYTIC DIGESTION; REACTION CYCLES; THERMOTOGA MARITIMA; TRANSITION STATE; TRANSMEMBRANE; WILSON DISEASE;

AMINES; AMINO ACIDS; BINDING ENERGY; BINDING SITES; CALCIUM; CONFORMATIONS; HEAVY METALS; ORGANIC ACIDS; PHOSPHORYLATION;

COPPER;

4 NITROPHENYLPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; CALCIUM; COPPER; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; PAPAIN;

AMINO ACID SEQUENCE; ARCHAEOGLOBUS FULGIDUS; ARTICLE; BACTERIUM MUTANT; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; TEMPERATURE DEPENDENCE; THERMOTOGA MARITIMA; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATALYSIS; CATION TRANSPORT PROTEINS; COPPER; GENETIC VARIATION; HEPATOLENTICULAR DEGENERATION; HUMANS; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; THERMOTOGA MARITIMA;

ARCHAEOGLOBUS FULGIDUS; THERMOTOGA MARITIMA;

EID: 66649083458     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900338n     Document Type: Article

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