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Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy.

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The PilQ secretin from the pathogenic bacterium Neisseria meningitidis is an integral outer membrane protein complex which plays a crucial role in the biogenesis of type IV pili. We present here the first three-dimensional structure of this type of secretin at 2.5-nm resolution, obtained by

Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure.

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PilQ is a member of the secretin family of outer membrane proteins and is specifically involved in secretion of type IV pili in Neisseria meningitidis, Neisseria gonorrhoeae, and Pseudomonas aeruginosa. The quaternary structure of PilQ from N. meningitidis was analyzed by transmission electron

Interaction with type IV pili induces structural changes in the bacterial outer membrane secretin PilQ.

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Type IV pili are cell surface organelles found on many Gram-negative bacteria. They mediate a variety of functions, including adhesion, twitching motility, and competence for DNA uptake. The type IV pilus is a helical polymer of pilin protein subunits and is capable of rapid polymerization or

The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity.

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The Pseudomonas secretin XcpQ forms an oligomeric complex, which is involved in the translocation of proteins across the outer membrane via the type II secretion pathway. Pseudomonas aeruginosa produces only small amounts of this complex, 50 to 100 copies per bacterium, and overexpression is lethal

Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy.

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Secretins, a superfamily of multimeric outer membrane proteins, mediate the transport of large macromolecules across the outer membrane of Gram-negative bacteria. Limited proteolysis of secretin PulD from the Klebsiella oxytoca pullulanase secretion pathway showed that it consists of an N-terminal

Idiopathic chronic pancreatitis in children: MR cholangiopancreatography after secretin administration.

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OBJECTIVE To assess the accuracy of dynamic magnetic resonance (MR) cholangiopancreatography after secretin administration in detecting pancreatic duct abnormalities typical of early-onset idiopathic chronic pancreatitis in children with recurrent episodes of idiopathic acute

Mucosal secretin content in postmortem tissues.

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Since human tissues are generally obtained at autopsy performed some hours after death, it is necessary to extrapolate from the observed concentration what the values might have been antemortem. In this study, we investigated the changes of secretin in gastrointestinal mucosa in man and rats under

Prospective evaluation of endoscopic ultrasonography, endoscopic retrograde pancreatography, and secretin test in the diagnosis of chronic pancreatitis.

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BACKGROUND Chronic pancreatitis in its early stages may defy diagnosis despite existing diagnostic modalities. Endoscopic retrograde pancreatography (ERCP), secretin test, and conventional ultrasound are insensitive in detecting the early stages of chronic pancreatitis. The aim of this study was to

Influence of secretin and caerulein on acid phosphatase activity in human saliva.

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Experimental studies have demonstrated a structural and functional correlation between the pancreas and salivary glands. Therefore, one may suppose that caerulein plus secretin, used in functional exploration of the exocrine pancreas, could exert an influence on acid phosphatase activity (AcP) and

Secretin PulD: association with pilot PulS, structure, and ion-conducting channel formation.

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The outer membrane protein PulD (secretin) of Klebsiella oxytoca is required for transport of pullulanase across this membrane. We have purified a multimeric PulD complex from an Escherichia coli strain expressing all the proteins involved in pullulanase secretion. The outer membrane-anchored

Structure and biochemical analysis of a secretin pilot protein.

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The ability to translocate virulence proteins into host cells through a type III secretion apparatus (TTSS) is a hallmark of several Gram-negative pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and enteropathogenic Escherichia coli. In common with other types of bacterial secretion

Structural characterization of the type-III pilot-secretin complex from Shigella flexneri.

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Assembly of the type-III secretion apparatus, which translocates proteins through both membranes of Gram-negative bacterial pathogens into host cells, requires the formation of an integral outer-membrane secretin ring. Typically, a small lipidated pilot protein is necessary for the stabilization and

Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution.

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The bacterial pathogen Neisseria meningitidis expresses long, thin, retractile fibers (called type IV pili) from its cell surface and uses these adhesive structures to mediate primary attachment to epithelial cells during host colonization and invasion. PilQ is an outer membrane protein complex that

A putative selectivity filter in the G-protein-coupled receptors for parathyroid hormone and secretion.

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The seven transmembrane segments (TMs) of many G-protein-coupled receptors (GPCRs) are thought to form a cavity into which cognate ligands insert, leading to receptor activation. Residues lining the cavity are often essential for optimal ligand binding and/or signal transduction. The present studies

Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.

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Type IV pili are polymeric fibers which protrude from the cell surface and play a critical role in adhesion and invasion by pathogenic bacteria. The secretion of pili across the periplasm and outer membrane is mediated by a specialized secretin protein, PilQ, but the way in which this large channel

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