The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

Nature Chemical Biology

Volumn 9, Issue 12, 2013, Pages 811-817

  Castro Roa, Daniel ^a   Garcia Pino, Abel ^b,c   De Gieter, Steven ^b,c   Van Nuland, Nico A J ^b,c   Loris, Remy ^b,c   Zenkin, Nikolay ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ELONGATION FACTOR TU; PROTEIN DOC; PROTEIN KINASE; TERNARY COMPLEX FACTOR; THREONINE; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL KINETICS; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RIBOSWITCH; RNA TRANSLATION; TRANSCRIPTION INITIATION;

ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; GUANOSINE TRIPHOSPHATE; MODELS, MOLECULAR; MUTATION; NUCLEOTIDYLTRANSFERASES; PEPTIDE ELONGATION FACTOR TU; PHOSPHORYLATION; PROTEIN FOLDING; RNA, TRANSFER;

BACTERIA (MICROORGANISMS);

EID: 84887997250     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1364     Document Type: Article

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