Novel structure of the N-terminal helical domain of BibA, a group B streptococcus immunogenic bacterial adhesin

Manne, K.; Chattopadhyay, D.; Agarwal, V.; Blom, A.M.; Khare, B.; Chakravarthy, S.; Chang, C.; Ton-That, H.; Narayana, S.V.L.

doi:10.1107/S2059798320008116

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
(a) A schematic of GBS BibA_34–400 with N-terminal His tag and TEV protease cleavage site. (b) SDS–PAGE gel showing the breakdown of the BibA_34–400 sample. The marker, BibA_34–400 without any mutations and BibA_34–400 with K49N, K70N and K112N mutations are labeled M, 1 and 2, respectively. (c) Picture of a BibA_126–398 crystal formed after proteolysis.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 76| Part 8| August 2020| Pages 759-770

https://doi.org/10.1107/S2059798320008116

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