6xxd

CryoEM structure of the type IV pilin PilA4 from Thermus thermophilusCryoEM structure of the type IV pilin PilA4 from Thermus thermophilus

Structural highlights

6xxd is a 16 chain structure with sequence from Thermus thermophilus HB27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.22Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PILA4_THET2 Plays an essential role in the assembly of two types of T4P pili: a wide and a narrow that participate in natural transformation and twitching motility (PubMed:32376942). Major component of the wide pilus that is essential for natural transformation working as a DNA translocator structure that spans the inner and outer membranes (PubMed:12839734, PubMed:16857013, PubMed:19396940, PubMed:32376942). In addition, participates in the assembly of the narrow pilus composed of the PilA5 subunit that is required for twitching motility (PubMed:32376942).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.

Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.,Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Friedrich A, Rumszauer J, Henne A, Averhoff B. Pilin-like proteins in the extremely thermophilic bacterium Thermus thermophilus HB27: implication in competence for natural transformation and links to type IV pilus biogenesis. Appl Environ Microbiol. 2003 Jul;69(7):3695-700. PMID:12839734 doi:10.1128/AEM.69.7.3695-3700.2003
↑ Rumszauer J, Schwarzenlander C, Averhoff B. Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. FEBS J. 2006 Jul;273(14):3261-72. PMID:16857013 doi:10.1111/j.1742-4658.2006.05335.x
↑ Schwarzenlander C, Haase W, Averhoff B. The role of single subunits of the DNA transport machinery of Thermus thermophilus HB27 in DNA binding and transport. Environ Microbiol. 2009 Apr;11(4):801-8. PMID:19396940 doi:10.1111/j.1462-2920.2008.01801.x
↑ Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942 doi:http://dx.doi.org/10.1038/s41467-020-15650-w
↑ Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942 doi:http://dx.doi.org/10.1038/s41467-020-15650-w

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OCA

[1] Friedrich A, Rumszauer J, Henne A, Averhoff B. Pilin-like proteins in the extremely thermophilic bacterium Thermus thermophilus HB27: implication in competence for natural transformation and links to type IV pilus biogenesis. Appl Environ Microbiol. 2003 Jul;69(7):3695-700. PMID:12839734 doi:10.1128/AEM.69.7.3695-3700.2003

[2] Rumszauer J, Schwarzenlander C, Averhoff B. Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. FEBS J. 2006 Jul;273(14):3261-72. PMID:16857013 doi:10.1111/j.1742-4658.2006.05335.x

[3] Schwarzenlander C, Haase W, Averhoff B. The role of single subunits of the DNA transport machinery of Thermus thermophilus HB27 in DNA binding and transport. Environ Microbiol. 2009 Apr;11(4):801-8. PMID:19396940 doi:10.1111/j.1462-2920.2008.01801.x

[4] Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942 doi:http://dx.doi.org/10.1038/s41467-020-15650-w

[5] Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942 doi:http://dx.doi.org/10.1038/s41467-020-15650-w

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