Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP

Cell Research

Volumn 23, Issue 6, 2013, Pages 775-787

  Yu, Qin ^a,b,d   Hu, Liyan ^b   Yao, Qing ^b   Zhu, Yongqun ^c   Dong, Na ^b   Wang, Da Cheng ^a   Shao, Feng ^b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b NATIONAL INSTITUTE OF BIOLOGICAL SCIENCES   (China)

^c ZHEJIANG UNIVERSITY   (China)

^d UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

GTPase activating protein (GAP); Legionella; Membrane trafficking; Rab GTPases; TBC GAP; Type IV secretion system

Indexed keywords

BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; ESPG PROTEIN, E COLI; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LEPB PROTEIN, LEGIONELLA PNEUMOPHILA; RAB PROTEIN;

ARTICLE; ENZYME ACTIVE SITE; GENETICS; LEGIONELLA PNEUMOPHILA; METABOLISM; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; GTPASE-ACTIVATING PROTEINS; LEGIONELLA PNEUMOPHILA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RAB1 GTP-BINDING PROTEINS;

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

EID: 84878709381     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2013.54     Document Type: Article

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