Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa type II secretion system
Identifieur interne : 000317 ( Main/Exploration ); précédent : 000316; suivant : 000318Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa type II secretion system
Auteurs : Laura P. Franz ; Badreddine Douzi ; Eric Durand ; David H. Dyer ; Romé Voulhoux ; Katrina T. ForestSource :
- Acta Crystallographica Section D [ 1399-0047 ] ; 2011-02-01.
English descriptors
Abstract
Pseudomonas aeruginosa utilizes the type II secretion machinery to transport virulence factors through the outer membrane into the extracellular space. Five proteins in the type II secretion system share sequence homology with pilin subunits of type IV pili and are called the pseudopilins. The major pseudopilin XcpTG assembles into an intraperiplasmic pilus and is thought to act in a piston‐like manner to push substrates through an outer membrane secretin. The other four minor pseudopilins, XcpUH, XcpVI, XcpWJ and XcpXK, play less well defined roles in pseudopilus formation. It was recently discovered that these four minor pseudopilins form a quaternary complex that is presumed to initiate the formation of the pseudopilus and to localize to its tip. Here, the structure of XcpWJ was refined to 1.85 Å resolution. The structure revealed the type IVa pilin fold with an embellished variable antiparallel β‐sheet as also found in the XcpWJ homologue enterotoxigenic Escherichia coli GspJW and the XcpUH homologue Vibrio cholerae EpsUH. It is proposed that the exposed surface of this sheet may cradle the long N‐terminal α1 helix of another pseudopilin. The final 31 amino acids of the XcpWJ structure are instrinsically disordered. Deletion of this unstructured region of XcpWJ did not prevent type II secretion in vivo.
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DOI: 10.1107/S0907444910051954
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Five proteins in the type II secretion system share sequence homology with pilin subunits of type IV pili and are called the pseudopilins. The major pseudopilin XcpTG assembles into an intraperiplasmic pilus and is thought to act in a piston‐like manner to push substrates through an outer membrane secretin. The other four minor pseudopilins, XcpUH, XcpVI, XcpWJ and XcpXK, play less well defined roles in pseudopilus formation. It was recently discovered that these four minor pseudopilins form a quaternary complex that is presumed to initiate the formation of the pseudopilus and to localize to its tip. Here, the structure of XcpWJ was refined to 1.85 Å resolution. The structure revealed the type IVa pilin fold with an embellished variable antiparallel β‐sheet as also found in the XcpWJ homologue enterotoxigenic Escherichia coli GspJW and the XcpUH homologue Vibrio cholerae EpsUH. It is proposed that the exposed surface of this sheet may cradle the long N‐terminal α1 helix of another pseudopilin. The final 31 amino acids of the XcpWJ structure are instrinsically disordered. Deletion of this unstructured region of XcpWJ did not prevent type II secretion in vivo.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Douzi, Badreddine" sort="Douzi, Badreddine" uniqKey="Douzi B" first="Badreddine" last="Douzi">Badreddine Douzi</name><name sortKey="Durand, Eric" sort="Durand, Eric" uniqKey="Durand E" first="Eric" last="Durand">Eric Durand</name><name sortKey="Dyer, David H" sort="Dyer, David H" uniqKey="Dyer D" first="David H." last="Dyer">David H. Dyer</name><name sortKey="Forest, Katrina T" sort="Forest, Katrina T" uniqKey="Forest K" first="Katrina T." last="Forest">Katrina T. Forest</name><name sortKey="Franz, Laura P" sort="Franz, Laura P" uniqKey="Franz L" first="Laura P." last="Franz">Laura P. Franz</name><name sortKey="Voulhoux, Rome" sort="Voulhoux, Rome" uniqKey="Voulhoux R" first="Romé" last="Voulhoux">Romé Voulhoux</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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