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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-1-23
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pubmed:abstractText |
The structural relatedness of pilins and the C-terminal half of adhesin proteins in different member species of Enterobacteriaceae was deduced from their two-dimensional sequence analysis using the hydrophobic cluster analysis (HCA) and secondary structure predictions from the profile network Hei-Delberg program (PHD). Despite a large evolutionary distance between the two protein families, we show that pilins and the C-terminal domain of adhesins have a similar folding that can serve as modules for pilus assembly.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
357
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
103-8
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pubmed:dateRevised |
2002-11-1
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pubmed:meshHeading |
pubmed-meshheading:8001668-Adhesins, Bacterial,
pubmed-meshheading:8001668-Amino Acid Sequence,
pubmed-meshheading:8001668-Bacterial Outer Membrane Proteins,
pubmed-meshheading:8001668-Enterobacteriaceae,
pubmed-meshheading:8001668-Fimbriae, Bacterial,
pubmed-meshheading:8001668-Fimbriae Proteins,
pubmed-meshheading:8001668-Molecular Sequence Data,
pubmed-meshheading:8001668-Protein Conformation,
pubmed-meshheading:8001668-Sequence Homology, Amino Acid
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pubmed:year |
1995
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pubmed:articleTitle |
Pilins of fimbrial adhesins of different member species of Enterobacteriaceae are structurally similar to the C-terminal half of adhesin proteins.
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pubmed:affiliation |
Laboratoire de Microbiologie, INRA, Centre de Recherches de Clermont-Ferrand-Theix, Saint-Genès-Champanelle, France.
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pubmed:publicationType |
Journal Article
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