Structural and functional analogy between pneumolysin and proaerolysin

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Structural and functional analogy between pneumolysin and proaerolysin. / Sowdhamini, R; Mitchell, T J; Andrew, P W; Morgan, P J.

In: Protein Engineering, Vol. 10, No. 3, 03.1997, p. 207-15.

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@article{1482ed2d55ed41168bccf87d0d058b0f,
title = "Structural and functional analogy between pneumolysin and proaerolysin",
abstract = "Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site-specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.",
keywords = "Amino Acid Sequence, Bacterial Proteins, Bacterial Toxins, Crystallography, X-Ray, Hemolysin Proteins, Microscopy, Electron, Models, Molecular, Molecular Sequence Data, Pore Forming Cytotoxic Proteins, Protein Conformation, Protein Folding, Protein Structure, Secondary, Sequence Alignment, Software, Streptolysins, Structure-Activity Relationship",
author = "R Sowdhamini and Mitchell, {T J} and Andrew, {P W} and Morgan, {P J}",
year = "1997",
month = mar,
language = "English",
volume = "10",
pages = "207--15",
journal = "Protein Engineering",
issn = "0269-2139",
publisher = "Oxford University Press",
number = "3",

}

RIS

TY - JOUR

T1 - Structural and functional analogy between pneumolysin and proaerolysin

AU - Sowdhamini, R

AU - Mitchell, T J

AU - Andrew, P W

AU - Morgan, P J

PY - 1997/3

Y1 - 1997/3

N2 - Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site-specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.

AB - Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site-specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.

KW - Amino Acid Sequence

KW - Bacterial Proteins

KW - Bacterial Toxins

KW - Crystallography, X-Ray

KW - Hemolysin Proteins

KW - Microscopy, Electron

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Pore Forming Cytotoxic Proteins

KW - Protein Conformation

KW - Protein Folding

KW - Protein Structure, Secondary

KW - Sequence Alignment

KW - Software

KW - Streptolysins

KW - Structure-Activity Relationship

M3 - Article

C2 - 9153085

VL - 10

SP - 207

EP - 215

JO - Protein Engineering

JF - Protein Engineering

SN - 0269-2139

IS - 3

ER -