TAILIEUCHUNG - Báo cáo khoa học: Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily

In Gram-negative bacteria, the two-partner secretion pathway mediates the secretion of TpsA proteins with various functions. TpsB transporters specifi-cally recognize their TpsA partners in the periplasm and mediate their trans-port through a hydrophilic channel. | Functional importance of a conserved sequence motif in FhaC a prototypic member of the TpsB Omp85 superfamily Anne-Sophie Delattre1-4 Bernard Clantin5 Nathalie Saint6 7 Camille Locht1-4 Vincent Villeret5 and Francoise Jacob-Dubuisson1-4 1 Inserm U1019 Center for Infection and Immunity of Lille France 2 Institut Pasteur de Lille France 3 Universite Lille Nord de France Lille France 4 CNRS UMR8204 Lille France 5 Institut de Recherche Interdisciplinaire USR3078 CNRS - Universite de Lille 1 et 2 Villeneuve d Ascq France 6 INSERM U554 Universite de Montpellier 1 et 2 France 7 UMR5048 CNRS Universite de Montpellier 1 et 2 France Keywords Bordetella outer membrane protein protein structure protein transport two-partner secretion Correspondence F. Jacob-Dubuisson 1 rue Calmette 59019 Lille Cedex France Fax 33 320 87 11 58 Tel 33 320 87 11 55 E-mail Database Structural data are available at the Protein Data Bank under the accession number 2QDZ FhaCWT Received 23 July 2010 revised 8 September 2010 accepted 13 September 2010 doi In Gram-negative bacteria the two-partner secretion pathway mediates the secretion of TpsA proteins with various functions. TpsB transporters specifically recognize their TpsA partners in the periplasm and mediate their transport through a hydrophilic channel. The filamentous haemagglutinin adhesin FHA ZFhaC pair represents a model two-partner secretion system with the structure of the TpsB transporter FhaC providing the bases to decipher the mechanism of action of these proteins. FhaC is composed of a b-barrel preceded by two periplasmic polypeptide-transport-associated POTRA domains in tandem. The barrel is occluded by an N-terminal helix and an extracellular loop L6 folded back into the FhaC channel. In this article we describe a functionally important motif of FhaC. The VRGY tetrad is highly conserved in the TpsB family and in FhaC it is located at the tip of L6 reaching the periplasm. .

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