5G24

Type IV-like pilin TTHA1219 from Thermus thermophilus

Summary for 5G24

• Entry DOI: 10.2210/pdb5g24/pdb
• Related: 5G23 5G25 5G2F
• Descriptor: TYPE-IV LIKE PILIN TTHA1219 (2 entities in total)
• Functional Keywords: structural protein, natural competence, type iv pilus, dna uptake
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 2
• Total formula weight: 50253.47

Authors

Karuppiah, V.,Derrick, J.P. (deposition date: 2016-04-06, release date: 2016-09-14, Last modification date: 2024-11-13)

Primary citation

Karuppiah, V.,Thistlethwaite, A.,Derrick, J.P.
Structures of Type Iv Pilins from Thermus Thermophilus Demonstrate Similarities with Type II Secretion System Pseudopilins
J.Struct.Biol., 196:375-, 2016

PubMed 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.

PubMed: 27612581
DOI: 10.1016/J.JSB.2016.08.006

Experimental method

X-RAY DIFFRACTION (2.3 Å)