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Novel structure of ...
Novel structure of the N-terminal helical domain of BibA, a group B streptococcus immunogenic bacterial adhesin
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- Manne, Kartik (author)
- University of Alabama
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- Chattopadhyay, Debasish (author)
- University of Alabama
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- Agarwal, Vaibhav (author)
- Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups
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- Blom, Anna M. (author)
- Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups
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- Khare, Baldeep (author)
- Purdue University
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- Chakravarthy, Srinivas (author)
- Illinois Institute of Technology
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- Chang, Chungyu (author)
- University of California, Los Angeles
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- Ton-That, Hung (author)
- University of California, Los Angeles
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- Narayana, Sthanam V.L. (author)
- University of Alabama
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(creator_code:org_t)
- 2020
- 2020
- English 12 s.
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In: Acta crystallographica. Section D, Structural biology. - 2059-7983. ; 76, s. 759-770
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Abstract
Subject headings
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- BibA, a group B streptococcus (GBS) surface protein, has been shown to protect the pathogen from phagocytic killing by sequestering a complement inhibitor: C4b-binding protein (C4BP). Here, the X-ray crystallographic structure of a GBS BibA fragment (BibA126-398) and a low-resolution small-angle X-ray scattering (SAXS) structure of the full-length N-terminal domain (BibA34-400) are described. The BibA126-398 fragment crystal structure displayed a novel and predominantly helical structure. The tertiary arrangement of helices forms four antiparallel three-helix-bundle-motif repeats, with one long helix from a bundle extending into the next. Multiple mutations on recombinant BibA34-400 delayed the degradation of the protein, and circular dichroism spectroscopy of BibA34-400 suggested a similar secondary-structure composition to that observed in the crystallized BibA126-398 fragment. A model was generated for the 92 N-terminal residues (BibA34-125) using structural similarity prediction programs, and a BibA34-400 model was generated by combining the coordinates of BibA34-126 and BibA126-398. The X-ray structure of BibA126-398 and the model of BibA34-400 fitted well into the calculated SAXS envelope. One possible binding site for the BibA N-terminal domain was localized to the N-terminal CCP (complement-control protein) domains of the C4BP α-chain, as indicated by the decreased binding of BibA to a ΔCCP1 C4BP α-chain mutant. In summary, it is suggested that the GBS surface protein BibA, which consists of three antiparallel α-helical-bundle motifs, is unique and belongs to a new class of Gram-positive surface adhesins.
Subject headings
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Keyword
- BibA
- C4b-binding proteins
- group B streptococcus
- immunogenic bacterial adhesins
- three-helix-bundle-motif repeats
Publication and Content Type
- art (subject category)
- ref (subject category)
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