Structural highlights
Function
PILA_MYXXD Major component of the type IV pili that are required for social gliding motility through cycles of extension and retraction. Extended pili are composed of thousands of copies of PilA and retract upon binding to extracellular polysaccharides and thereby pull the cell forward.[1] [2] [3] [4]
Publication Abstract from PubMed
Type IV pili (T4P) are ubiquitous bacterial cell surface filaments important for surface motility, adhesion to biotic and abiotic surfaces, DNA uptake, biofilm formation, and virulence. T4P are built from thousands of copies of the major pilin subunit and tipped by a complex composed of minor pilins and in some systems also the PilY1 adhesin. While the major pilins of structurally characterized T4P have lengths of up to 161 residues, the major pilin PilA of Myxococcus xanthus is unusually large with 208 residues. All major pilins have a highly conserved N-terminal domain and a highly variable C-terminal domain, and the additional residues in the M. xanthus PilA are due to a larger C-terminal domain. We solved the structure of the M. xanthus T4P (T4P (Mx) ) at a resolution of 3.0 A using cryo-electron microscopy (cryo-EM). The T4P (Mx) follows the structural blueprint observed in other T4P with the pilus core comprised of the extensively interacting N-terminal alpha1-helices while the globular domains decorate the T4P surface. The atomic model of PilA built into this map shows that the large C-terminal domain has much more extensive intersubunit contacts than major pilins in other T4P. As expected from these greater contacts, the bending and axial stiffness of the T4P (Mx) is significantly higher than that of other T4P and supports T4P-dependent motility on surfaces of different stiffnesses. Notably, T4P (Mx) variants with interrupted intersubunit interfaces had decreased bending stiffness and strongly reduced motility on all surfaces. These observations support an evolutionary scenario whereby the large major pilin enables the formation of a rigid T4P that expands the environmental conditions in which the T4P system functions.
Large pilin subunits provide distinct structural and mechanical properties for the Myxococcus xanthus type IV pilus.,Treuner-Lange A, Zheng W, Viljoen A, Lindow S, Herfurth M, Dufrene YF, Sogaard-Andersen L, Egelman EH bioRxiv. 2023 Jul 22:2023.07.22.550172. doi: 10.1101/2023.07.22.550172. Preprint. PMID:37503255[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang Z, Lux R, Hu W, Hu C, Shi W. PilA localization affects extracellular polysaccharide production and fruiting body formation in Myxococcus xanthus. Mol Microbiol. 2010 Jun;76(6):1500-13. PMID:20444090 doi:10.1111/j.1365-2958.2010.07180.x
- ↑ Yang Z, Hu W, Chen K, Wang J, Lux R, Zhou ZH, Shi W. Alanine 32 in PilA is important for PilA stability and type IV pili function in Myxococcus xanthus. Microbiology (Reading). 2011 Jul;157(Pt 7):1920-1928. PMID:21493683 doi:10.1099/mic.0.049684-0
- ↑ Wu SS, Kaiser D. Genetic and functional evidence that Type IV pili are required for social gliding motility in Myxococcus xanthus. Mol Microbiol. 1995 Nov;18(3):547-58. PMID:8748037 doi:10.1111/j.1365-2958.1995.mmi_18030547.x
- ↑ Wu SS, Kaiser D. Regulation of expression of the pilA gene in Myxococcus xanthus. J Bacteriol. 1997 Dec;179(24):7748-58. PMID:9401034 doi:10.1128/jb.179.24.7748-7758.1997
- ↑ Treuner-Lange A, Zheng W, Viljoen A, Lindow S, Herfurth M, Dufrêne YF, Søgaard-Andersen L, Egelman EH. Large pilin subunits provide distinct structural and mechanical properties for the Myxococcus xanthus type IV pilus. bioRxiv. 2023 Jul 22:2023.07.22.550172. PMID:37503255 doi:10.1101/2023.07.22.550172