ArticleThe Biochemical journal2013
Structure and mechanism of the PilF DNA transformation ATPase from Thermus thermophilus.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022Review
- Natural transformation in Gram-negative bacteria thriving in extreme environments: from genes and genomes to proteins, structures and regulation.Extremophiles : life under extreme conditions · 2021Review
- Cyclic-di-GMP and ADP bind to separate domains of PilB as mutual allosteric effectors.The Biochemical journal · 2020Article
- Article
- The Dynamic Structures of the Type IV Pilus.Microbiology spectrum · 2019Review
- The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili fromFEBS open bio · 2019Article
- Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly.Scientific reports · 2018Article
- Functional dissection of the three N-terminal general secretory pathway domains and the Walker motifs of the traffic ATPase PilF from Thermus thermophilus.Extremophiles : life under extreme conditions · 2018Article
- Cyclic Di-GMP Binding by an Assembly ATPase (PilB2) and Control of Type IV Pilin Polymerization in the Gram-Positive Pathogen Clostridium perfringens.Journal of bacteriology · 2017Article
- Complete Genome Analysis ofFrontiers in microbiology · 2017Article
- Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins.Journal of structural biology · 2016Article
- Article
- Zinc and ATP binding of the hexameric AAA-ATPase PilF from Thermus thermophilus: role in complex stability, piliation, adhesion, twitching motility, and natural transformation.The Journal of biological chemistry · 2014Article
- Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL.Journal of structural biology · 2014Article
- Assembly of the respiratory mucin MUC5B: a new model for a gel-forming mucin.The Journal of biological chemistry · 2014Article
- Type IV pilus biogenesis, twitching motility, and DNA uptake in Thermus thermophilus: discrete roles of antagonistic ATPases PilF, PilT1, and PilT2.Applied and environmental microbiology · 2014Article
- Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity.Structure (London, England : 1993) · 2013Article
- The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content.Extremophiles : life under extreme conditions · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Many Gram-negative bacteria contain specific systems for uptake of foreign DNA, which play a critical role in the acquisition of antibiotic resistance. The TtPilF (PilF ATPase from Thermus thermophilus) is required for high transformation efficiency, but its mechanism of action is unknown. In the present study, we show that TtPilF is able to bind to both DNA and RNA. The structure of TtPilF was determined by cryoelectron microscopy in the presence and absence of the ATP analogue p[NH]ppA (adenosine 5'-[β,γ-imido]triphosphate), at 10 and 12 Å (1 Å=0.1 nm) resolutions respectively. It consists of two distinct N- and C-terminal regions, separated by a short stem-like structure. Binding of p[NH]ppA induces structural changes in the C-terminal domains, which are transmitted via the stem to the N-terminal domains. Molecular models were generated for the apoenzyme and p[NH]ppA-bound states in the C-terminal regions by docking of a model based on a crystal structure from a closely related enzyme. Analysis of DNA binding by electron microscopy, using gold labelling, localized the binding site to the N-terminal domains. The results suggest a model in which DNA uptake by TtPilF is powered by ATP hydrolysis, causing conformational changes in the C-terminal domains, which are transmitted via the stem to take up DNA into the cell.
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