对TpsB/Omp85超家族的首次结构洞察。

First structural insights into the TpsB/Omp85 superfamily.

作者信息

Jacob-Dubuisson Françoise, Villeret Vincent, Clantin Bernard, Delattre Anne-Sophie, Saint Nathalie

机构信息

INSERM U629, Institut Pasteur de Lille, 1 rue Calmette, F-59019 Lille cedex, France.

出版信息

Biol Chem. 2009 Aug;390(8):675-84. doi: 10.1515/BC.2009.099.

DOI:10.1515/BC.2009.099

PMID:19558323

Abstract

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 super-family.

摘要

TpsB/Omp85超家族的蛋白质参与革兰氏阴性菌外膜的蛋白质转运或组装，其远缘真核生物亲属在叶绿体和线粒体中发挥类似功能。一种TpsB转运蛋白FhaC的X射线结构为解读这些蛋白质的作用机制提供了依据。FhaC在周质中有两个POTRA结构域、一个跨膜β桶和一个含有功能重要基序的大环，体现了该超家族的保守特征。