Sökning: onr:"swepub:oai:lup.lub.lu.se:6ae81574-7cce-45c2-8461-fc4950250ced" >
Novel structure of ...
Novel structure of the N-terminal helical domain of BibA, a group B streptococcus immunogenic bacterial adhesin
-
- Manne, Kartik (författare)
- University of Alabama
-
- Chattopadhyay, Debasish (författare)
- University of Alabama
-
- Agarwal, Vaibhav (författare)
- Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups
-
visa fler...
-
- Blom, Anna M. (författare)
- Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups
-
- Khare, Baldeep (författare)
- Purdue University
-
- Chakravarthy, Srinivas (författare)
- Illinois Institute of Technology
-
- Chang, Chungyu (författare)
- University of California, Los Angeles
-
- Ton-That, Hung (författare)
- University of California, Los Angeles
-
- Narayana, Sthanam V.L. (författare)
- University of Alabama
-
visa färre...
-
(creator_code:org_t)
- 2020
- 2020
- Engelska 12 s.
-
Ingår i: Acta crystallographica. Section D, Structural biology. - 2059-7983. ; 76, s. 759-770
- Relaterad länk:
-
http://dx.doi.org/10...
-
visa fler...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Nyckelord
- BibA
- C4b-binding proteins
- group B streptococcus
- immunogenic bacterial adhesins
- three-helix-bundle-motif repeats
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
Hitta via bibliotek
Till lärosätets databas