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Structural analysis of Efb, a fibrinogen binding protein of Staphylococcus aureus

Wade, D (author)
Palma, M (author)
Flock, J I (author)
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Berndt, Kurt D (author)
Karolinska Institutet
Silberring, J (author)
Galaktionov, S G (author)
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 (creator_code:org_t)
1998
1998
English.
In: Protein peptide letters. - 0929-8665 .- 1875-5305. ; 5:4, s. 199-206
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Staphylococcus aureus produces and secretes a small, basic protein, designated Efb, that binds to fibrinogen and seems to be required for virulence of the organism. A 3D model of Efb was developed, and it predicts that the C-terminal half of the protein contains substantial alpha-helical content. CD analysis of Efb yielded a value of 40-41% alpha-helix. Calcium and zinc both influence the interactions between Efb and fibrinogen, and an analysis of the amino acid sequence of Efb revealed the presence of consensus sequences for the binding of both metals.

Subject headings

NATURVETENSKAP  -- Biologi -- Strukturbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Structural Biology (hsv//eng)

Keyword

circular-dichroism
coordination
prediction
virulence
zinc

Publication and Content Type

ref (subject category)
art (subject category)

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Wade, D
Palma, M
Flock, J I
Berndt, Kurt D
Silberring, J
Galaktionov, S G
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NATURAL SCIENCES
NATURAL SCIENCES
and Biological Scien ...
and Structural Biolo ...
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Protein peptide ...
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Södertörn University

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