ArticleJournal of molecular biology2012
Structure of an essential type IV pilus biogenesis protein provides insights into pilus and type II secretion systems.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Type IV pili ofEcoSal Plus · 2024Review
- Cryo-EM Structure of the Type IV Pilus Extension ATPase from Enteropathogenic Escherichia coli.mBio · 2022Article
- Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022Review
- Multiple conformations facilitate PilT function in the type IV pilus.Nature communications · 2019Article
- A CAZyme-Rich Genome of a Taxonomically Novel Rhodophyte-Associated Carrageenolytic Marine Bacterium.Marine biotechnology (New York, N.Y.) · 2018Article
- Predicting and Interpreting the Structure of Type IV Pilus of Electricigens by Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2017Article
- Complex N acquisition by soil diazotrophs: how the ability to release exoenzymes affects N fixation by terrestrial free-living diazotrophs.The ISME journal · 2017Article
- Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.The Journal of biological chemistry · 2016Article
- PilN Binding Modulates the Structure and Binding Partners of the Pseudomonas aeruginosa Type IVa Pilus Protein PilM.The Journal of biological chemistry · 2016Article
- The Type IV Pilus Assembly ATPase PilB of Myxococcus xanthus Interacts with the Inner Membrane Platform Protein PilC and the Nucleotide-binding Protein PilM.The Journal of biological chemistry · 2016Article
- Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment Subcomplex Mutations.Journal of bacteriology · 2015Article
- Editorial.FEMS microbiology reviews · 2015Article
- Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives.FEMS microbiology reviews · 2015Review
- 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
- Redefining the PF06864 Pfam family based on Burkholderia pseudomallei PilO2(Bp) S-SAD crystal structure.PloS one · 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
- Type IV pili in Gram-positive bacteria.Microbiology and molecular biology reviews : MMBR · 2013Review
- Secretion of TcpF by the Vibrio cholerae toxin-coregulated pilus biogenesis apparatus requires an N-terminal determinant.Journal of bacteriology · 2013Article
- PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA.Journal of bacteriology · 2013Article
- Insights into FlaI functions in archaeal motor assembly and motility from structures, conformations, and genetics.Molecular cell · 2013Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Type IV pili (T4Ps) are long cell surface filaments, essential for microcolony formation, tissue adherence, motility, transformation, and virulence by human pathogens. The enteropathogenic Escherichia coli bundle-forming pilus is a prototypic T4P assembled and powered by BfpD, a conserved GspE secretion superfamily ATPase held by inner-membrane proteins BfpC and BfpE, a GspF-family membrane protein. Although the T4P assembly machinery shares similarity with type II secretion (T2S) systems, the structural biochemistry of the T4P machine has been obscure. Here, we report the crystal structure of the two-domain BfpC cytoplasmic region (N-BfpC), responsible for binding to ATPase BfpD and membrane protein BfpE. The N-BfpC structure reveals a prominent central cleft between two α/β-domains. Despite negligible sequence similarity, N-BfpC resembles PilM, a cytoplasmic T4P biogenesis protein. Yet surprisingly, N-BfpC has far greater structural similarity to T2S component EpsL, with which it also shares virtually no sequence identity. The C-terminus of the cytoplasmic domain, which leads to the transmembrane segment not present in the crystal structure, exits N-BfpC at a positively charged surface that most likely interacts with the inner membrane, positioning its central cleft for interactions with other Bfp components. Point mutations in surface-exposed N-BfpC residues predicted to be critical for interactions among BfpC, BfpE, and BfpD disrupt pilus biogenesis without precluding interactions with BfpE and BfpD and without affecting BfpD ATPase activity. These results illuminate the relationships between T4P biogenesis and T2S systems, imply that subtle changes in component residue interactions can have profound effects on function and pathogenesis, and suggest that T4P systems may be disrupted by inhibitors that do not preclude component assembly.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.