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CryoEM structure of Myxococcus xanthus type IV pilusCryoEM structure of Myxococcus xanthus type IV pilus
Structural highlights
FunctionPILA_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 PubMedType IVa pili (T4aP) are ubiquitous cell surface filaments important for surface motility, adhesion to surfaces, DNA uptake, biofilm formation, and virulence. T4aP 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 major pilins of structurally characterized T4aP have lengths of <165 residues, the major pilin PilA of Myxococcus xanthus is unusually large with 208 residues. All major pilins have a conserved N-terminal domain and a variable C-terminal domain, and the additional residues of PilA are due to a larger C-terminal domain. We solved the structure of the M. xanthus T4aP (T4aP(Mx)) at a resolution of 3.0 A using cryo-EM. The T4aP(Mx) follows the structural blueprint of other T4aP with the pilus core comprised of the interacting N-terminal alpha1-helices, while the globular domains decorate the T4aP surface. The atomic model of PilA built into this map shows that the large C-terminal domain has more extensive intersubunit contacts than major pilins in other T4aP. As expected from these greater contacts, the bending and axial stiffness of the T4aP(Mx) is significantly higher than that of other T4aP and supports T4aP-dependent motility on surfaces of different stiffnesses. Notably, T4aP(Mx) variants with interrupted intersubunit interfaces had decreased bending stiffness, pilus length, and strongly reduced motility. These observations support an evolutionary scenario whereby the large major pilin enables the formation of a rigid T4aP that expands the environmental conditions in which the T4aP system functions. Tight-packing of large pilin subunits provides distinct structural and mechanical properties for the Myxococcus xanthus type IVa pilus.,Treuner-Lange A, Zheng W, Viljoen A, Lindow S, Herfurth M, Dufrene YF, Sogaard-Andersen L, Egelman EH Proc Natl Acad Sci U S A. 2024 Apr 23;121(17):e2321989121. doi: , 10.1073/pnas.2321989121. Epub 2024 Apr 16. PMID:38625941[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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