3INO

1.95A Resolution Structure of Protective Antigen Domain 4

3INO の概要

• エントリーDOI: 10.2210/pdb3ino/pdb
• 分子名称: Protective antigen PA-63 (2 entities in total)
• 機能のキーワード: anthrax, domain 4, protective antigen, toxin, calcium, cleavage on pair of basic residues, metal-binding, plasmid, secreted, virulence, immune system
• 由来する生物種: Bacillus anthracis (anthrax,anthrax bacterium)
• 細胞内の位置: Secreted, extracellular space: P13423
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32484.51

構造登録者

Lovell, S.,Williams, A.S.,Anbanandam, A.,El-Chami, R.,Bann, J.G. (登録日: 2009-08-12, 公開日: 2009-11-03, 最終更新日: 2023-09-06)

主引用文献

Williams, A.S.,Lovell, S.,Anbanandam, A.,El-Chami, R.,Bann, J.G.
Domain 4 of the anthrax protective antigen maintains structure and binding to the host receptor CMG2 at low pH
Protein Sci., 18:2277-2286, 2009

PubMed Abstract: Domain 4 of the anthrax protective antigen (PA) plays a key role in cellular receptor recognition as well as in pH-dependent pore formation. We present here the 1.95 A crystal structure of domain 4, which adopts a fold that is identical to that observed in the full-length protein. We have also investigated the structural properties of the isolated domain 4 as a function of pH, as well as the pH-dependence on binding to the von Willebrand factor A domain of capillary morphogenesis protein 2 (CMG2). Our results provide evidence that the isolated domain 4 maintains structure and interactions with CMG2 at pH 5, a pH that is known to cause release of the receptor on conversion of the heptameric prepore (PA(63))(7) to a membrane-spanning pore. Our results suggest that receptor release is not driven solely by a pH-induced unfolding of domain 4.

PubMed: 19722284
DOI: 10.1002/pro.238

実験手法

X-RAY DIFFRACTION (1.95 Å)