Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

Holmgren, Anders; Brändén, Carl‐Ivar

doi:10.1038/342248a0

Cited by 293 publications

(203 citation statements)

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“…The immmunoglobulin fold appears to be a typical example of a three-dimensional motif compatible with a large variety of sequences, even when canonical Cys residues are absent [16,30,32,45,461. The immunoglobulin fold is widespread, and is involved in events governing immune recognition (immunoglobulins, T cell receptor, etc) and interactions between cells (CD4, CDS, CD2, LFA3, etc) [45].…”

Section: Discussionmentioning

confidence: 99%

“…This strand would be necessary for the return of the polypeptide chain towards the small domain and to the stem (by analogy with the hemagglutinin head structure, which otherwise possesses an eight-strand fold). Eight-strand structures of such immunoglobulin domains, such as chaperone papD, have been reported [32]. On this basis, we built a model of the bovine leukemia virus envelope head on the HLA-A2 a3 template [29] (Fig.…”

Section: Analysis Of the Head Of The Bovine Leukemia Virus Envelope Gmentioning

confidence: 99%

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Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data

Callebaut

Portetelle

Burny

et al. 1994

European Journal of Biochemistry

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Sequence analysis using the sensitive hydrophobic cluster analysis method shows that the bovine leukemia virus envelope glycoproteins conserve the general organization of the influenza hemagglutinin into a 'stem', containing the external part of the transmembrane glycoprotein and the Nterminal and C-terminal parts of the external glycoprotein, and a 'head', containing only external glycoprotein residues. However, our analysis suggests, for the first time, that the bovine leukemia virus envelope head will not adopt the typical 'jelly-roll' fold of the influenza A hemagglutinin head, but most likely folds into another type of 'Greek-key' structure corresponding to the overall topology of constant immunoglobulin domains. We constructed a three-dimensional model for the bovine leukemia virus envelope head by homology modeling using the crystal structure of the human histocompatibility antigen HLA-A2 a3 domain. Furthermore, we propose a general model for the oligomeric organization of this head, based on the hemagglutinin trimer. The proposed structural organization of bovine leukemia virus external glycoprotein is further supported by antipeptide and monoclonal antibody reactivities. Our modeling study suggests that the loops of the two neutralizing peptides located in the head are adjacent at the top of the domain and define a potential interaction site of the external glycoprotein with its cellular receptor. This site is topologically similar to the binding site of hemagglutinin with its cellular receptor, sialic acid. The other neutralizing peptides are located within a small domain linking the head to the stem.These data are of interest for defining other oncoviral glycoproteins heads and receptor-binding sites.

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Section: Discussionmentioning

confidence: 99%

Section: Analysis Of the Head Of The Bovine Leukemia Virus Envelope Gmentioning

confidence: 99%

Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data

Callebaut

Portetelle

Burny

et al. 1994

European Journal of Biochemistry

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“…P pilus assembly requires the function of a dedicated chaperone (PapD) (11,12) and the usher (PapC) (3,13). The P pilus comprises a flexible-tip fibrillum made up of minor pilins with the two-domain adhesin PapG at the distal end where it can recognize Galα1-4Gal disaccharide-containing glycolipids found in the human kidney (14,15).…”

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confidence: 99%

Molecular basis of usher pore gating in Escherichia coli pilus biogenesis

Volkan

Kalas

Pinkner³

et al. 2013

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

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Extracellular fibers called chaperone-usher pathway pili are critical virulence factors in a wide range of Gram-negative pathogenic bacteria that facilitate binding and invasion into host tissues and mediate biofilm formation. Chaperone-usher pathway ushers, which catalyze pilus assembly, contain five functional domains: a 24-stranded transmembrane β-barrel translocation domain (TD), a β-sandwich plug domain (PLUG), an N-terminal periplasmic domain, and two Cterminal periplasmic domains (CTD1 and 2). Pore gating occurs by a mechanism whereby the PLUG resides stably within the TD pore when the usher is inactive and then upon activation is translocated into the periplasmic space, where it functions in pilus assembly. Using antibiotic sensitivity and electrophysiology experiments, a single salt bridge was shown to function in maintaining the PLUG in the TD channel of the P pilus usher PapC, and a loop between the 12th and 13th beta strands of the TD (β12-13 loop) was found to facilitate pore opening. Mutation of the β12-13 loop resulted in a closed PapC pore, which was unable to efficiently mediate pilus assembly. Deletion of the PapH terminator/anchor resulted in increased OM permeability, suggesting a role for the proper anchoring of pili in retaining OM integrity. Further, we introduced cysteine residues in the PLUG and N-terminal periplasmic domains that resulted in a FimD usher with a greater propensity to exist in an open conformation, resulting in increased OM permeability but no loss in type 1 pilus assembly. These studies provide insights into the molecular basis of usher pore gating and its roles in pilus biogenesis and OM permeability.outer membrane usher | macromolecular assembly | bacterial pathogenesis

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“…The chaperone consists of two immunoglobulin (Ig)-like domains (11). In the periplasm, each pilus subunit forms an incomplete Ig fold in which the C-terminal ␤-strand is absent.…”

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confidence: 99%

Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry

Rose

Verger

Daviter

et al. 2008

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

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P pili are multisubunit fibers essential for the attachment of uropathogenic Escherichia coli to the kidney. These fibers are formed by the noncovalent assembly of six different homologous subunit types in an array that is strictly defined in terms of both the number and order of each subunit type. Assembly occurs through a mechanism termed ''donor-strand exchange (DSE)'' in which an N-terminal extension (Nte) of one subunit donates a ␤-strand to an adjacent subunit, completing its Ig fold. Despite structural determination of the different subunits, the mechanism determining specificity of subunit ordering in pilus assembly remained unclear. Here, we have used noncovalent mass spectrometry to monitor DSE between all 30 possible pairs of P pilus subunits and their Ntes. We demonstrate a striking correlation between the natural order of subunits in pili and their ability to undergo DSE in vitro. The results reveal insights into the molecular mechanism by which subunit ordering during the assembly of this complex is achieved.donor strand exchange ͉ electrospray ionization ͉ noncovalent protein complexes ͉ uropathogenic bacteria

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Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

Abstract: The chaperone protein PapD mediates assembly of pili in Escherichia coli. Its polypeptide chain folds into two immunoglobulin-type domains that are homologous in sequence to the human lymphocyte differentiation antigen Leu-1/CD5.

Cited by 293 publications

References 21 publications

Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data

Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data

Molecular basis of usher pore gating in Escherichia coli pilus biogenesis

Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry

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