The inner membrane subassembly of the enteropathogenic <i>Escherichia coli</i> bundle‐forming pilus machine

Milgotina, Ekaterina; Lieberman, Joshua A.; Donnenberg, Michael S.

doi:10.1111/j.1365-2958.2011.07771.x

Cited by 9 publications

(14 citation statements)

References 3 publications

(3 reference statements)

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“…Abendroth et al determined the crystal structure of a complex between the N-terminal domain of the T2SS ATPase EpsE and the cytoplasmic domain of EpsL (40), which is similar in structure to PilM (11). In addition, BfpC, a key protein in the biogenesis of type IVb bundle forming pili, shares structural similarity with EpsL and PilM (41) and binds to its cognate assembly ATPase, BfpD (40,42). Interestingly, both the cytoplasmic and periplasmic domains of EpsL form dimers (24,43), raising the question of how this is consistent with binding to the hexameric EpsE ATPase (44).…”

Section: Discussionmentioning

confidence: 99%

Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis

Karuppiah

Collins

Thistlethwaite

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Significance Type IV pili are long, thin fibers, formed mainly of polymers of a single pilin protein, which are displayed on the surfaces of many bacteria, including several human pathogens. Here, we report three-dimensional reconstructions of the PilMNO inner membrane complex, alone and in complex with pilin protein, through a combination of X-ray crystallography and electron microscopy. PilMNO forms a dimeric T-shaped structure, binding two copies of the pilin protein at its extremities. The results provide a structural model for the way in which pilin is harvested from the inner membrane and made available to other components of the type IV pilus biogenesis machinery.

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Section: Discussionmentioning

confidence: 99%

Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis

Karuppiah

Collins

Thistlethwaite

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…This arrangement of the inner and outer membrane components of the pilus assembly complex may provide an unobstructed path through the periplasm, including the peptidoglycan, for the assembled pilus. Also, hypothesized interactions of PilM with the platform protein PilC, as demonstrated for orthologs in the T2SS and the T4bP system (30)(31)(32), would connect the cytoplasmic motor with the outer membrane secretin, allowing for the efficient transmission of the signals that control its opening and closing.…”

Section: Discussionmentioning

confidence: 99%

PilMNOPQ from the Pseudomonas aeruginosa Type IV Pilus System Form a Transenvelope Protein Interaction Network That Interacts with PilA

et al. 2013

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“…24 BfpD is a member of the highly conserved PilB/GspEhexamericsecretion ATPase superfamily, whose members act in many bacterial and archaeal macromolecular transport systems, such as Type II secretion (T2S), type IV secretion, DNA uptake by natural transformation and conjugation, and archaeal flagellar assembly systems. 25 BfpE is a member of the GspF secretion family of membrane proteins, which are conserved in T4P, T2S, and Gram-positive competence systems, with recognizable orthologs in archaeal flagellar systems.…”

Section: Introductionmentioning

confidence: 99%

Structure of an Essential Type IV Pilus Biogenesis Protein Provides Insights into Pilus and Type II Secretion Systems

Yamagata¹,

Milgotina²,

Scanlon³

et al. 2012

Journal of Molecular Biology

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Type IV pili (T4Ps) are long cell surface filaments, essential for microcolony formation, tissue adherence, motility, transformation, and virulence by human pathogens. The enteropathogenic E. colibundle-forming pilus (BFP) is a prototypic T4P assembled and powered by BfpD, a conserved GspE secretion superfamily ATPase held by inner membrane proteins BfpC andBfpE, 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 greaterstructural 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 donot preclude component assembly.

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The inner membrane subassembly of the enteropathogenic Escherichia coli bundle‐forming pilus machine

Cited by 9 publications

References 3 publications

Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis

Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis

PilMNOPQ from the Pseudomonas aeruginosa Type IV Pilus System Form a Transenvelope Protein Interaction Network That Interacts with PilA

Structure of an Essential Type IV Pilus Biogenesis Protein Provides Insights into Pilus and Type II Secretion Systems

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