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Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors.

Solanki V, Kapoor S, Thakur KG
FEBS J 285 3402-3421 (2018)
Cited: 12 times
EuropePMC logo PMID: 30066435

Abstract

Type IVa pili are bacterial appendages involved in diverse physiological processes, including electron transfer in Geobacter sulfurreducens. ATP hydrolysis coupled with conformational changes powers the extension (PilB) and retraction (PilT) motors in the pilus machinery. We report the unliganded crystal structures of the core ATPase domain of PilB and PilT-4 from G. sulfurreducens at 3.1 and 2.6 Å resolution, respectively. PilB structure revealed three distinct conformations, that is, open, closed, and open' which were previously proposed to be mediated by ATP/ADP binding. PilT-4 subunits, on the other hand, were observed in the closed state conformation. We further report that both PilB and PilT-4 hexamers have two high-affinity ATP-binding sites. Comparative structural analysis and solution data presented here supports the "symmetric rotary model" for these ATPase motors. Our data further suggest that pores of these motors rotate either clockwise or counterclockwise to facilitate assembly or disassembly of right-handed or left-handed pilus.

Articles - 5zfr mentioned but not cited (2)

  1. Structural insights into the mechanism of Type IVa pilus extension and retraction ATPase motors. Solanki V, Kapoor S, Thakur KG. FEBS J 285 3402-3421 (2018)
  2. Cryo-EM Structure of the Type IV Pilus Extension ATPase from Enteropathogenic Escherichia coli. Nayak AR, Singh PK, Zhao J, Samsó M, Donnenberg MS. mBio 13 e0227022 (2022)


Reviews citing this publication (4)

  1. Type IV pili: dynamics, biophysics and functional consequences. Craig L, Forest KT, Maier B. Nat Rev Microbiol 17 429-440 (2019)
  2. DNA Uptake by Type IV Filaments. Piepenbrink KH. Front Mol Biosci 6 1 (2019)
  3. Landmark Discoveries and Recent Advances in Type IV Pilus Research. Singh PK, Little J, Donnenberg MS. Microbiol Mol Biol Rev 86 e0007622 (2022)
  4. Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask). Pelicic V. Microbiology (Reading) 169 (2023)

Articles citing this publication (6)

  1. The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase. Adams DW, Pereira JM, Stoudmann C, Stutzmann S, Blokesch M. PLoS Genet 15 e1008393 (2019)
  2. Multiple conformations facilitate PilT function in the type IV pilus. McCallum M, Benlekbir S, Nguyen S, Tammam S, Rubinstein JL, Burrows LL, Howell PL. Nat Commun 10 5198 (2019)
  3. Cyclic-di-GMP and ADP bind to separate domains of PilB as mutual allosteric effectors. Dye KJ, Yang Z. Biochem J 477 213-226 (2020)
  4. High-Throughput Screen for Inhibitors of the Type IV Pilus Assembly ATPase PilB. Dye KJ, Vogelaar NJ, Sobrado P, Yang Z. mSphere 6 e00129-21 (2021)
  5. The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri. Llontop EE, Cenens W, Favaro DC, Sgro GG, Salinas RK, Guzzo CR, Farah CS. PLoS Pathog 17 e1009808 (2021)
  6. Generation of High Current Densities in Geobacter sulfurreducens Lacking the Putative Gene for the PilB Pilus Assembly Motor. Ueki T, Walker DJF, Nevin KP, Ward JE, Woodard TL, Nonnenmann SS, Lovley DR. Microbiol Spectr 9 e0087721 (2021)


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