5B2H

Crystal structure of HA33 from Clostridium botulinum serotype C strain Yoichi

Summary for 5B2H

• Entry DOI: 10.2210/pdb5b2h/pdb
• Descriptor: HA-33, TRIETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: hemagglutinin, sugar binding protein
• Biological source: Clostridium botulinum
• Total number of polymer chains: 2
• Total formula weight: 65842.90

Authors

Akiyama, T.,Hayashi, S.,Matsumoto, T.,Hasegawa, K.,Yamano, A.,Suzuki, T.,Niwa, K.,Watanabe, T.,Sagane, Y.,Yajima, S. (deposition date: 2016-01-15, release date: 2016-06-15, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)