The Legionella pneumophila GTPase activating protein LepB accelerates Rab1 deactivation by a non-canonical hydrolytic mechanism

Journal of Biological Chemistry

Volumn 288, Issue 33, 2013, Pages 24000-24011

  Mishra, Ashwini K ^a   Del Campo, Claudia M ^a   Collins, Robert E ^a,c   Roy, Craig R ^b   Lambright, David G ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC NETWORKS; FINGER MECHANISMS; GTP HYDROLYSIS; GTPASE-ACTIVATING PROTEIN; HYDROLYTIC MECHANISMS; LEGIONELLA PNEUMOPHILA; RAB GTPASES; SELECTIVE PRESSURE;

BIOCHEMISTRY; BIOLOGY;

HYDROLYSIS;

ALUMINUM FLUORIDE; ARGININE; GLUTAMIC ACID; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; PROTEIN LEPB; RAB PROTEIN; RAB1A PROTEIN; RAB3A PROTEIN; RAS PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CARCINOGENICITY; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DXXGQ MOTIF; ENZYME SPECIFICITY; LEGIONELLA PNEUMOPHILA; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN HYDROLYSIS; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS;

GAP; GTPASE; GTPASE ACTIVATING PROTEIN; HOST-PATHOGEN INTERACTIONS; LEGIONELLA PNEUMOPHILA; LEPB; RAB; RAB PROTEINS; RAB1; X-RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; GTP PHOSPHOHYDROLASES; GTPASE-ACTIVATING PROTEINS; GUANOSINE TRIPHOSPHATE; HUMANS; HYDROLYSIS; KINETICS; LEGIONELLA PNEUMOPHILA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RAB GTP-BINDING PROTEINS; SEQUENCE ALIGNMENT; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

EID: 84882408124     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.470625     Document Type: Article

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