Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic Ra...
Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP
About this item
Full title
Author / Creator
Yu, Qin , Hu, Liyan , Yao, Qing , Zhu, Yongqun , Dong, Na , Wang, Da-Cheng and Shao, Feng
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
Rab GTPases are emerging targets of diverse bacterial pathogens. Here, we perform biochemical and structural analyses of LepB, a Rab GTPase-activating protein （GAP） effector from Legionellapneumophila. We map LepB GAP domain to residues 313-618 and show that the GAP domain is Rabl specific with a catalytic activity higher than the canonical eukaryo...
Alternative Titles
Full title
Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3674391
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3674391
Other Identifiers
ISSN
1001-0602
E-ISSN
1748-7838
DOI
10.1038/cr.2013.54
