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Crystallization and preliminary X‐ray analysis of a novel haemagglutinin component of the toxin complex of serotype C Clostridium botulinum
Author(s) -
Hayashi Shintaro,
Akiyama Tomonori,
Sagane Yoshimasa,
Miyashita ShinIchiro,
Watanabe Toshihiro,
Yajima Shunsuke,
Niwa Koichi
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14003094
Subject(s) - serotype , clostridium botulinum , escherichia coli , microbiology and biotechnology , chemistry , strain (injury) , crystallization , toxin , biochemistry , biology , gene , organic chemistry , anatomy
The botulinum toxin complex, the causative agent of botulism, passes through the intestinal wall via sugar‐chain‐dependent cell binding of a haemagglutinin of 33 kDa molecular weight (HA‐33). The amino‐acid sequence of the C‐terminal half of HA‐33 of the serotype C strain Yoichi (C‐Yoichi) shares only 46% identity with those of the major serotype C strains. Additionally, C‐Yoichi HA‐33 exhibits a unique sugar‐binding specificity. In the present work, C‐Yoichi HA‐33 was expressed in Escherichia coli and crystallized. Diffraction data were collected at a resolution of 2.2 Å. The crystals belonged to space group R 3. The complete detailed protein structure will yield insight into how the unique HA‐33 protein recognizes sugar moieties.