First structural insights into the TpsB/Omp85 superfamily

被引：56
作者：
Jacob-Dubuisson, Francoise [1 ,2 ]
Villeret, Vincent [2 ,3 ]
Clantin, Bernard [2 ,3 ]
Delattre, Anne-Sophie [1 ,2 ]
Saint, Nathalie [4 ,5 ]
机构：
[1] Inst Pasteur, INSERM, U629, F-59019 Lille, France
[2] Inst Pasteur, IFR142, F-59019 Lille, France
[3] Univ Lille Nord France, Inst Biol Lille, UMR8161, Inst Pasteur Lille, F-59021 Lille, France
[4] Univ Montpellier 1 & 2, INSERM, U554, F-34090 Montpellier, France
[5] Univ Montpellier 1 & 2, CNRS, UMR5048, F-34090 Montpellier, France
来源：
BIOLOGICAL CHEMISTRY | 2009年 / 390卷 / 08期
关键词：
beta barrel protein; outer membrane; POTRA domain; protein secretion; two-partner secretion; PERTUSSIS FILAMENTOUS HEMAGGLUTININ; 2-PARTNER SECRETION PATHWAY; BARREL MEMBRANE-PROTEINS; BACTERIAL OUTER-MEMBRANE; ESCHERICHIA-COLI; FUNCTIONAL DOMAINS; CRYSTAL-STRUCTURE; OMP85; FAMILY; PORE; FHAC;
D O I：
10.1515/BC.2009.099
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Proteins of the TpsB/Omp85 superfamily are involved in protein transport across, or assembly into, the outer membrane of Gram-negative bacteria, and their distant eukaryotic relatives exert similar functions in chloroplasts and mitochondria. The X-ray structure of one TpsB transporter, FhaC, provides the bases to decipher the mechanisms of action of these proteins. With two POTRA domains in the periplasm, a transmembrane beta barrel and a large loop harboring a functionally important motif, FhaC epitomizes the conserved features of the superfamily.
引用
收藏
页码：675 / 684
页数：10
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