The Receptor Binding Protein P2 of PRD1, a Virus Targeting Antibiotic-Resistant Bacteria, Has a Novel Fold Suggesting Multiple Functions

Xu, Lan; Benson, Stacy D.; Butcher, Sarah J.; Bamford, Dennis H.; Burnett, Roger M.

doi:10.1016/s0969-2126(03)00023-6

Cited by 45 publications

(40 citation statements)

References 72 publications

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“…Furthermore, the PRD1 P3 fold is similar to that of adenovirus hexon (2,(5)(6)(7)(8). In addition, in both viruses, the stability of the capsid is secured by minor cementing proteins (9)(10)(11)(12), and the receptor-recognition complexes are composed of elongated spikes attached to the pentameric vertex proteins (3,(12)(13)(14)(15).…”

mentioning

confidence: 87%

“…The low-resolution SAXS models of the full-length P5 and the collagenase-resistant fragment complement the x-ray structure (28). On the basis of the x-ray structure, the spike protein P2 is an elongated monomer with a head and a tail domain (15). The head has a pseudo-␤-propeller fold, and the tail is an extended ␤-sheet.…”

mentioning

confidence: 90%

“…The head has a pseudo-␤-propeller fold, and the tail is an extended ␤-sheet. The head domain has been suggested to be distal to the virion and responsible for receptor binding (15).…”

mentioning

confidence: 99%

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Tale of two spikes in bacteriophage PRD1

Huiskonen

Manole

Butcher

2007

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

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Structural comparisons between bacteriophage PRD1 and adenovirus have revealed an evolutionary relationship that has contributed significantly to current ideas on virus phylogeny. However, the structural organization of the receptor-binding spike complex and how the different symmetry mismatches are mediated between the spike-complex proteins are not clear. We determined the architecture of the PRD1 spike complex by using electron microscopy and three-dimensional image reconstruction of a series of PRD1 mutants. We constructed an atomic model for the fulllength P5 spike protein by using comparative modeling. P5 was shown to be bound directly to the penton base protein P31. P5 and the receptor-binding protein P2 form two separate spikes, interacting with each other near the capsid shell. P5, with a tumor necrosis factor-like head domain, may have been responsible for host recognition before capture of the current receptor-binding protein P2.electron cryomicroscopy ͉ symmetry mismatch ͉ vertex ͉ virus

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confidence: 87%

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confidence: 90%

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Tale of two spikes in bacteriophage PRD1

Huiskonen

Manole

Butcher

2007

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

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“…Monomeric receptor binding protein P2 (Grahn et al, 1999 andXu et al, 2003) was expressed as a fusion protein in a monomeric form ( Fig. 2A).…”

Section: Solubility and Multimericity Of Viral Fluorescent Fusion Promentioning

confidence: 99%

“…In PRD1, the capsid is mainly composed of the major capsid protein P3, which forms pseudohexameric trimers Benson et al, 1999). The receptor binding spike complex at the virion vertices contains the pentameric penton protein P31 forming the base structure from which the trimeric spike protein P5 and the monomeric receptor binding protein P2 protrude , Merckel et al, 2005, Rydman et al, 1999and Xu et al, 2003. The spike structure complex is stabilized by the integral membrane protein P16 linking the vertex to the underlying viral membrane (Jaatinen et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

Karttunen¹,

Mäntynen²,

Ihalainen³

et al. 2014

Virus Research

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Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their localization in living cells by confocal microscopy, indicated that multimeric PRD1 proteins were prone to localize in the cell poles. Furthermore, PRD1 spike complex proteins P5 and P31, as fusion proteins, were shown to be functional in the virion assembly. In addition, they were shown to co-localize in the specific polar area of the cells, which might have a role in the multimerization and formation of viral protein complexes.

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Conformational changes in redox pairs of protein structures

et al. 2009

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Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox-active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox-active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox-active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox-activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.

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The Receptor Binding Protein P2 of PRD1, a Virus Targeting Antibiotic-Resistant Bacteria, Has a Novel Fold Suggesting Multiple Functions

Cited by 45 publications

References 72 publications

Tale of two spikes in bacteriophage PRD1

Tale of two spikes in bacteriophage PRD1

Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

Conformational changes in redox pairs of protein structures

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