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Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins

DOI: 10.1016/j.jsb.2016.08.006 DOI Help

Authors: Vijaykumar Karuppiah (University of Manchester) , Angela Thistlethwaite (University of Manchester) , Jeremy P. Derrick (The University of Manchester)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Structural Biology , VOL 196 , PAGES 375 – 384

State: Published (Approved)
Published: December 2016

Open Access Open Access

Abstract: Type IV pilins are proteins which form polymers that extend from the surface of the bacterial cell; they are involved in mediating a wide variety of functions, including adhesion, motility and natural competence. Here we describe the determination of the crystal structures of three type IVa pilins proteins from the thermophile Thermus thermophilus. They form part of a cluster of pilus-like proteins within the genome; our results show that one, Tt1222, is very closely related to the main structural type IV pilin, PilA4. The other two, Tt1218 and Tt1219, also adopt canonical pilin-like folds but, interestingly, are most closely related to the structures of the type II secretion system pseudopilins, EpsI/GspI and XcpW/GspJ. GspI and GspJ have been shown to form a complex with another pseudopilin, GspK, and this heterotrimeric complex is known to play a key role in initiating assembly of a pseudopilus which is thought to drive the secretion process. The structural similarity of Tt1218 and Tt1219 to GspI and GspJ suggests that they might work in a similar way, to deliver functions associated with type IV pili in T. thermophilus, such as natural competence.

Journal Keywords: Pilus; Type II secretion system; X-ray crystallography; Thermophile; Natural competence

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography