Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain

EMBO Journal

Volumn 32, Issue 10, 2013, Pages 1469-1477

  Campanacci, Valérie ^a   Mukherjee, Shaeri ^b   Roy, Craig R ^b   Cherfils, Jacqueline ^a  

^a LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Ankyrin repeats; FIC domain; Legionella; Phosphocholination; Rab GTPase

Indexed keywords

ANKX PROTEIN; ANKYRIN; BACTERIAL PROTEIN; CITICOLINE; CYTIDINE PHOSPHATE; PHOSPHORYLCHOLINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; LEGIONELLA PNEUMOPHILA; MEMBRANE TRANSPORT; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

ANKYRIN REPEAT; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; LEGIONELLA PNEUMOPHILA; MODELS, MOLECULAR; PHOSPHORYLCHOLINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

BACTERIA (MICROORGANISMS); EUKARYOTA; LEGIONELLA; LEGIONELLA PNEUMOPHILA;

EID: 84878644184     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2013.82     Document Type: Article

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