Crystallization and preliminary X‐ray analysis of a novel haemagglutinin component of the toxin complex of serotype C Clostridium botulinum. Issue 3 (1st March 2014)

• Record Type: Journal Article
• Authors: Hayashi, Shintaro; Akiyama, Tomonori; Sagane, Yoshimasa; Miyashita, Shin‐Ichiro; Watanabe, Toshihiro; Yajima, Shunsuke; Niwa, Koichi
• Is Part Of: Acta crystallographica. Volume 70:Issue 3(2014:Mar.)
• Page Start: 370
• Page End: 373
• Publication Date: 2014-03-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14003094
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The botulinum toxin complex, the causative agent of botulism, passes through the intestinal wall <italic>via</italic> 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 <italic>Escherichia coli</italic> and crystallized. Diffraction data were collected at a resolution of 2.2 Å. The crystals belonged to space group <italic>R</italic>3. The complete detailed protein structure will yield insight into how the unique HA‐33 protein recognizes sugar moieties.</p> </abstract>