Engineering and characterization of the ribosomal L10-L12 stalk complex A structural element responsible for high turnover of the elongation factor g-dependent GTPase

Journal of Biological Chemistry

Volumn 284, Issue 1, 2009, Pages 85-92

  Miyoshi, Tomohiro ^a   Nomura, Takaomi ^b   Uchiumi, Toshio ^a  

^a NIIGATA UNIVERSITY   (Japan)

^b SHINSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BINDING SITES; ELECTRIC FIELD EFFECTS; ESCHERICHIA COLI; PROTEINS;

C-TERMINAL DOMAIN (CTD); E. COLI; ELONGATION FACTORS; GTPASE ACTIVITY; HYBRID SYSTEM (HS); N TERMINAL DOMAIN (NTD); PENTAMERIC COMPLEX; TRANSLATION FACTORS;

PORT TERMINALS;

CHIMERIC PROTEIN; ELONGATION FACTOR G; GUANOSINE TRIPHOSPHATASE; PROTEIN L 12; PROTEIN L10; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; RIBOSOME; THERMUS THERMOPHILUS;

BACTERIAL PROTEINS; ESCHERICHIA COLI; MULTIPROTEIN COMPLEXES; PEPTIDE ELONGATION FACTOR G; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RIBOSOMAL PROTEINS; RIBOSOMES; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

EID: 58649124104     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M806024200     Document Type: Article

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