Structure of the Pseudomonas aeruginosa Type IVa Pilus Secretin at 7.4 Å

Koo, Jarley; Lamers, Ryan P.; Rubinstein, John L.; Burrows, Lori L.; Howell, P. Lynne

doi:10.1016/j.str.2016.08.007

Cited by 42 publications

(45 citation statements)

References 75 publications

(110 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2a). The OM secretin subcomplex includes PilQ, a multimeric OM pore protein through which the growing pilus is assembled and disassembled [65][66][67][68] , and the pilotin protein The final structural component completing the T4P system is the helical pilus filament, composed of major and minor pilin subunits and adhesin molecules 81,82 (FIG. 2d).…”

Section: T4p Biogenesismentioning

confidence: 99%

See 1 more Smart Citation

A comprehensive guide to pilus biogenesis in Gram-negative bacteria

2017

View full text Add to dashboard Cite

Pili are critical virulence factors of many Gram-negative pathogens. These surface structures provide bacteria with a link to their outside environments, allowing bacteria to interact with their hosts, other surfaces or with each other. They can even provide a conduit for the exchange of information. The surface chemistries and other biophysical properties of pili are uniquely adapted to the environmental challenges faced by bacteria. The assembly of these surface structures presents a molecular engineering challenge, which bacteria have solved in a variety of unique ways. In this review, we examine recent advances in our structural understanding of various Gram-negative pilus systems and discuss their functional implications.

show abstract

Section: T4p Biogenesismentioning

confidence: 99%

“…Recently, a ~7.4 Å cryo-EM structure of the P. aeruginosa secretin pore was determined 67 (FIG. 2c).…”

Section: Structure Of T4p Machinerymentioning

confidence: 99%

A comprehensive guide to pilus biogenesis in Gram-negative bacteria

2017

View full text Add to dashboard Cite

show abstract

“…Combining biochemistry, imaging, and reprojections, low-resolution cryo-EM images produced for PulD from Klebsiella (9), GspD from Vibrio (10), or PilQ from Neisseria at 12 Å (11) contributed to provide a rough but rational model of a saucer-like complex with gate properties which would sit in the outer membrane. However, the long-awaited higher resolution at 7.4 Å was first glimpsed by the impatient scientific community only in 2016 with a study on the Pseudomonas aeruginosa PilQ T4P secretin (12). A few months later, the 3.6-Å structure of the Salmonella enterica InvG T3SS secretin was published (PDB accession number 5TCQ) ( Fig.…”

mentioning

confidence: 99%

Multiple Structures Disclose the Secretins' Secrets

Filloux

Voulhoux

2018

J Bacteriol

View full text Add to dashboard Cite

Bacterial secretins are outer membrane proteins that provide a path for secreted proteins to access the cell exterior/surface. They are one of the core components of secretion machines and are found in type II and type III secretion systems (T2SS and T3SS, respectively). The secretins comprise giant ring-shaped homooligomers whose precise atomic organization was only recently deciphered thanks to spectacular developments in cryo-electron microscopy (cryo-EM) imaging techniques.

show abstract

“…The PilQ complex is highly dynamic and undergoes major conformational changes by opening and closing two periplasmic gates . PilQ of T. thermophilus differs from all known secretins, which contain only 2–4 rings and only one gate . The elongation of the PilQ complex might be an adaptation to the wide periplasm of T. thermophilus .…”

mentioning

confidence: 99%

The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili from Thermus thermophilus

2018

View full text Add to dashboard Cite

A major driving force for the adaptation of bacteria to changing environments is the uptake of naked DNA from the environment by natural transformation, which allows the acquisition of new capabilities. Uptake of the high molecular weight DNA is mediated by a complex transport machinery that spans the entire cell periphery. This DNA translocator catalyzes the binding and splitting of double‐stranded DNA and translocation of single‐stranded DNA into the cytoplasm, where it is recombined with the chromosome. The thermophilic bacterium Thermus thermophilus exhibits the highest transformation frequencies reported and is a model system to analyze the structure and function of this macromolecular transport machinery. Transport activity is powered by the traffic ATPase PilF, a soluble protein that forms hexameric complexes. Here, we demonstrate that PilF physically binds to an inner membrane assembly platform of the DNA translocator, comprising PilMNO, via the ATP‐binding protein PilM. Binding to PilMNO or PilMN stimulates the ATPase activity of PilF ~ 2‐fold, whereas there is no stimulation when binding to PilM or PilN alone. A PilM K26A variant defective in ATP binding still binds PilF and, together with PilN, stimulates PilF‐mediated ATPase activity. PilF is unique in having three conserved GSPII (general secretory pathway II) domains (A–C) at its N terminus. Deletion analyses revealed that none of the GSPII domains is essential for binding PilMN, but GSPIIC is essential for PilMN‐mediated stimulation of ATP hydrolysis by PilF. Our data suggest that PilM is a coupling protein that physically and functionally connects the soluble motor ATPase PilF to the DNA translocator via the PilMNO assembly platform.

show abstract

Structure of the Pseudomonas aeruginosa Type IVa Pilus Secretin at 7.4 Å

Cited by 42 publications

References 75 publications

A comprehensive guide to pilus biogenesis in Gram-negative bacteria

A comprehensive guide to pilus biogenesis in Gram-negative bacteria

Multiple Structures Disclose the Secretins' Secrets

The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili from Thermus thermophilus

Contact Info

Product

Resources

About