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Assembly of the Type II Secretion System such as Found in Vibrio cholerae Depends on the Novel Pilotin AspS
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نویسنده
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dunstan r.a. ,heinz e. ,wijeyewickrema l.c. ,pike r.n. ,purcell a.w. ,evans t.j. ,praszkier j. ,robins-browne r.m. ,strugnell r.a. ,korotkov k.v. ,lithgow t.
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منبع
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plos pathogens - 2013 - دوره : 9 - شماره : 1
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چکیده
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The type ii secretion system (t2ss) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. a key element in the machinery is the secretin: an integral,multimeric outer membrane protein that forms the secretion pore. we show that three distinct forms of t2sss can be distinguished based on the sequence characteristics of their secretin pores. detailed comparative analysis of two of these,the klebsiella-type and vibrio-type,showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. we have determined the crystal structure of the novel pilotin asps from vibrio cholerae,demonstrating convergent evolution wherein asps is functionally equivalent and yet structurally unrelated to the pilotins found in klebsiella and other bacteria. asps binds to a specific targeting sequence in the vibrio-type secretins,enhances the kinetics of secretin assembly,and homologs of asps are found in all species of vibrio as well those few strains of escherichia and shigella that have acquired a vibrio-type t2ss. © 2013 dunstan et al.
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آدرس
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department of biochemistry and molecular biology,monash university,melbourne, Australia, department of biochemistry and molecular biology,monash university,melbourne,australia,victorian bioinformatics consortium,monash university,melbourne, Australia, department of biochemistry and molecular biology,monash university,melbourne, Australia, department of biochemistry and molecular biology,monash university,melbourne, Australia, department of biochemistry and molecular biology,monash university,melbourne, Australia, department of molecular and cellular biochemistry and center for structural biology,university of kentucky,lexington,ky, United States, department of microbiology and immunology,the university of melbourne,melbourne,australia,monash institute of medical research,melbourne, Australia, department of microbiology and immunology,the university of melbourne,melbourne,australia,murdoch childrens research institute,royal children's hospital,melbourne, Australia, department of microbiology and immunology,the university of melbourne,melbourne, Australia, department of molecular and cellular biochemistry and center for structural biology,university of kentucky,lexington,ky, United States, department of biochemistry and molecular biology,monash university,melbourne, Australia
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Authors
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