The long α-helix of SecA is important for the ATPase coupling of translocation

Journal of Biological Chemistry

Volumn 281, Issue 47, 2006, Pages 36249-36256

  Mori, Hiroyuki ^a   Ito, Koreaki ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; ENZYME KINETICS; PROTEINS;

HELICAL SCAFFOLD DOMAIN (HSD); LIGAND-ACTIVATED ATPASE ENGINE; PREPROTEIN TRANSLOCATION;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; AMINO ACID; ARGININE; CYSTEINE; DISULFIDE; GLUTAMIC ACID; PROTEIN SECA; TRANSLOCON;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHROMOSOME TRANSLOCATION; CONTROLLED STUDY; DISULFIDE BOND; GENE MUTATION; GENETIC CONSERVATION; ION TRANSPORT; MOTOR PERFORMANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; UPREGULATION;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CYSTEINE; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; LIGANDS; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT;

EID: 33845999952     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M606906200     Document Type: Article

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