Structural Basis for Translocation of a Biofilm-supporting   Exopolysaccharide across the Bacterial Outer Membrane

doi:10.1074/jbc.M115.711762

CORC > 北京大学 > 生命科学学院

	Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane
	Wang, Yan ; Pannuri, Archana Andole ; Ni, Dongchun ; Zhou, Haizhen ; Cao, Xiou ; Lu, Xiaomei ; Romeo, Tony ; Huang, Yihua
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2016
关键词	ACETYLGLUCOSAMINE SURFACE POLYSACCHARIDE ESCHERICHIA-COLI PSEUDOMONAS-AERUGINOSA MOLECULAR-DYNAMICS PROTEIN ADHESIN POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE PGAABCD MATRIX CSRA
DOI	10.1074/jbc.M115.711762
英文摘要	The partially de-N-acetylated poly-beta-1,6-N-acetyl-D-glucosamine (dPNAG) polymer serves as an intercellular biofilm adhesin that plays an essential role for the development and maintenance of integrity of biofilms of diverse bacterial species. Translocation of dPNAG across the bacterial outer membrane is mediated by a tetratricopeptide repeat-containing outer membrane protein, PgaA. To understand the molecular basis of dPNAG translocation, we determined the crystal structure of the C-terminal transmembrane domain of PgaA (residues 513807). The structure reveals that PgaA forms a 16-strand trans membrane beta-barrel, closed by four loops on the extracellular surface. Half of the interior surface of the barrel that lies parallel to the translocation pathway is electronegative, suggesting that the corresponding negatively charged residues may assist the secretion of the positively charged dPNAG polymer. In vivo complementation assays in a pgaA deletion bacterial strain showed that a cluster of negatively charged residues proximal to the periplasm is necessary for biofilm formation. Biochemical analyses further revealed that the tetratricopeptide repeat domain of PgaA binds directly to the N-deacetylase PgaB and is critical for biofilm formation. Our studies support a model in which the positively charged PgaB-bound dPNAG polymer is delivered to PgaA through the PgaA-PgaB interaction and is further targeted to the beta-barrel lumen of PgaA potentially via a charge complementarity mechanism, thus priming the translocation of dPNAG across the bacterial outer membrane.; National Institutes of Health [GM059969, GM066794]; National Natural Science Foundation of China [31470743, 31170698]; Ministry of Science and Technology (China) "973" Project [2013CB910603, 2012CB917302]; Chinese Academy of Sciences [XDB08020302]; University of Florida CHRIS Project [FLA-MCS-004949]; SCI(E); EI; PubMed; ARTICLE; tromeo@ufl.edu; yihuahuang@sun5.ibp.ac.cn; 19; 10046-10057; 291
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/434571]
专题	生命科学学院
推荐引用方式 GB/T 7714	Wang, Yan,Pannuri, Archana Andole,Ni, Dongchun,et al. Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016.
APA	Wang, Yan.,Pannuri, Archana Andole.,Ni, Dongchun.,Zhou, Haizhen.,Cao, Xiou.,...&Huang, Yihua.(2016).Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane.JOURNAL OF BIOLOGICAL CHEMISTRY.
MLA	Wang, Yan,et al."Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane".JOURNAL OF BIOLOGICAL CHEMISTRY (2016).