5B2H

Crystal structure of HA33 from Clostridium botulinum serotype C strain Yoichi

5B2H の概要

• エントリーDOI: 10.2210/pdb5b2h/pdb
• 分子名称: HA-33, TRIETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: hemagglutinin, sugar binding protein
• 由来する生物種: Clostridium botulinum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65842.90

構造登録者

Akiyama, T.,Hayashi, S.,Matsumoto, T.,Hasegawa, K.,Yamano, A.,Suzuki, T.,Niwa, K.,Watanabe, T.,Sagane, Y.,Yajima, S. (登録日: 2016-01-15, 公開日: 2016-06-15, 最終更新日: 2023-11-08)

主引用文献

Sagane, Y.,Hayashi, S.,Akiyama, T.,Matsumoto, T.,Hasegawa, K.,Yamano, A.,Suzuki, T.,Niwa, K.,Watanabe, T.,Yajima, S.
Conformational divergence in the HA-33/HA-17 trimer of serotype C and D botulinum toxin complex
Biochem.Biophys.Res.Commun., 476:280-285, 2016

PubMed Abstract: Clostridium botulinum produces a large toxin complex (L-TC) comprising botulinum neurotoxin associated with auxiliary nontoxic proteins. A complex of 33- and 17-kDa hemagglutinins (an HA-33/HA-17 trimer) enhances L-TC transport across the intestinal epithelial cell layer via binding HA-33 to a sugar on the cell surface. At least two subtypes of serotype C/D HA-33 exhibit differing preferences for the sugars sialic acid and galactose. Here, we compared the three-dimensional structures of the galactose-binding HA-33 and HA-33/HA-17 trimers produced by the C-Yoichi strain. Comparisons of serotype C/D HA-33 sequences reveal a variable region with relatively low sequence similarity across the C. botulinum strains; the variability of this region may influence the manner of sugar-recognition by HA-33. Crystal structures of sialic acid- and galactose-binding HA-33 are broadly similar in appearance. However, small-angle X-ray scattering revealed distinct solution structures for HA-33/HA-17 trimers. A structural change in the C-terminal variable region of HA-33 might cause a dramatic shift in the conformation and sugar-recognition mode of HA-33/HA-17 trimer.

PubMed: 27237978
DOI: 10.1016/j.bbrc.2016.05.113

実験手法

X-RAY DIFFRACTION (2.2 Å)