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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1997-8-8
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0269-2139
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-15
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9153085-Amino Acid Sequence,
pubmed-meshheading:9153085-Bacterial Proteins,
pubmed-meshheading:9153085-Bacterial Toxins,
pubmed-meshheading:9153085-Crystallography, X-Ray,
pubmed-meshheading:9153085-Hemolysin Proteins,
pubmed-meshheading:9153085-Microscopy, Electron,
pubmed-meshheading:9153085-Models, Molecular,
pubmed-meshheading:9153085-Molecular Sequence Data,
pubmed-meshheading:9153085-Pore Forming Cytotoxic Proteins,
pubmed-meshheading:9153085-Protein Conformation,
pubmed-meshheading:9153085-Protein Folding,
pubmed-meshheading:9153085-Protein Structure, Secondary,
pubmed-meshheading:9153085-Sequence Alignment,
pubmed-meshheading:9153085-Software,
pubmed-meshheading:9153085-Streptolysins,
pubmed-meshheading:9153085-Structure-Activity Relationship
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pubmed:year |
1997
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pubmed:articleTitle |
Structural and functional analogy between pneumolysin and proaerolysin.
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pubmed:affiliation |
Imperial Cancer Research Fund, Unit of Structural Molecular Biology, Department of Crystallography, Birkbeck College, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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