Crystal structure of the ternary FimC-FimFt-FimDNcomplex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD
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چکیده
منابع مشابه
Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD.
Adhesive type 1 pili from uropathogenic Escherichia coli are filamentous protein complexes that are attached to the assembly platform FimD in the outer membrane. During pilus assembly, FimD binds complexes between the chaperone FimC and type 1 pilus subunits in the periplasm and mediates subunit translocation to the cell surface. Here we report nuclear magnetic resonance and X-ray protein struc...
متن کاملDissection of Pilus Tip Assembly by the FimD Usher Monomer
Type 1 pili are representative of a class of bacterial surface structures assembled by the conserved chaperone/usher pathway and used by uropathogenic Escherichia coli to attach to bladder cells during infection. The outer membrane assembly platform-the usher-is critical for the formation of pili, catalysing the polymerisation of pilus subunits and enabling the secretion of the nascent pilus. D...
متن کاملRecognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis.
In this work we discover that a specific recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is essential for the biogenesis of type 1 pili in Escherichia coli. These filamentous organelles are assembled by the chaperone-usher pathway, in which binary complexes between fimbrial subunits and the periplasmic chaperone FimC are recognized by the outer membrane protein Fim...
متن کاملThe usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events.
Pilus biogenesis on the surface of uropathogenic Escherichia coli requires the chaperone/usher pathway, a terminal branch of the general secretory pathway. In this pathway, periplasmic chaperone-subunit complexes target an outer membrane (OM) usher for subunit assembly into pili and secretion to the cell surface. The molecular mechanisms of protein secretion across the OM are not well understoo...
متن کاملThe Role of Chaperone-subunit Usher Domain Interactions in the Mechanism of Bacterial Pilus Biogenesis Revealed by ESI-MS*
The PapC usher is a β-barrel outer membrane protein essential for assembly and secretion of P pili that are required for adhesion of pathogenic E. coli, which cause the development of pyelonephritis. Multiple protein subunits form the P pilus, the highly specific assembly of which is coordinated by the usher. Despite a wealth of structural knowledge, how the usher catalyzes subunit polymerizati...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2008
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2008.01.030