Journal ArticleDOI
Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.
Michael W. Parker,J T Buckley,J. P. M. Postma,Alec D. Tucker,Kevin Leonard,Franc Pattus,Demetrius Tsernoglou +6 more
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TLDR
The structure of proaerolysin determined by X-ray crystallography at 2.8 Å resolution is described and it is proposed that insertion of the protein into lipid bilayers to form ion channels is accounted for.Abstract:
Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 A resolution. The protoxin (M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels.read more
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Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore
TL;DR: The structure proves the heptameric subunit stoichiometry of the α-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of β barrel pore-forming toxins.
Journal ArticleDOI
The C-type lectin-like domain superfamily
Alex N. Zelensky,Jill E. Gready +1 more
TL;DR: The superfamily of proteins containing C‐type lectin‐like domains (CTLDs) is a large group of extracellular Metazoan proteins with diverse functions that have evolved to specifically recognize protein, lipid and inorganic ligands, including the vertebrate clade‐specific snake venoms, and fish antifreeze and bird egg‐shell proteins.
Journal ArticleDOI
Structure and function of bacterial outer membrane proteins: barrels in a nutshell
TL;DR: The outer membrane protects Gram‐negative bacteria against a harsh environment and the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction.
Journal ArticleDOI
Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria.
TL;DR: Results show that oligomeric Bax possesses channel-forming activity whereas monomeric P-40 and n-dedecyl maltoside have no such activity.
Journal ArticleDOI
Pore-forming toxins: ancient, but never really out of fashion
TL;DR: The diverse pore architectures and membrane insertion mechanisms that have been revealed by structural studies of PFTs are discussed, and how these features contribute to binding specificity for different membrane targets are considered.
References
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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
Wolfgang Kabsch,Chris Sander +1 more
TL;DR: A set of simple and physically motivated criteria for secondary structure, programmed as a pattern‐recognition process of hydrogen‐bonded and geometrical features extracted from x‐ray coordinates is developed.
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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The Protein Data Bank: a computer-based archival file for macromolecular structures.
Frances C. Bernstein,Thomas F. Koetzle,Graheme J. B. Williams,Edgar F. Meyer,Michael D. Brice,John R. Rodgers,O. Kennard,Takehiko Shimanouchi,Mitsuo Tasumi +8 more
TL;DR: The Protein Data Bank is a computer-based archival file for macromolecular structures that stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies.
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A graphics model building and refinement system for macromolecules
TL;DR: A model building and refinement system is described for use with a Vector General 3400 display that has been used to assist in difference Fourier map interpretation at medium and high resolution, and to build a protein molecule into a multiple isomorphous replacement phased electron density map.
Journal ArticleDOI
Crystal structures explain functional properties of two E. coli porins
S. W. Cowan,Tilman Schirmer,Gabriele Rummel,Matthias Steiert,Robin Ghosh,Richard A. Pauptit,Johan N. Jansonius,Jurg P. Rosenbusch +7 more
TL;DR: The crystal structures of matrix porin and phosphoporin both reveal trimers of identical subunits, each subunit consisting of a 16-stranded anti-parallel β-barrel containing a pore.