3INO
1.95A Resolution Structure of Protective Antigen Domain 4
Summary for 3INO
Entry DOI | 10.2210/pdb3ino/pdb |
Descriptor | Protective antigen PA-63 (2 entities in total) |
Functional Keywords | anthrax, domain 4, protective antigen, toxin, calcium, cleavage on pair of basic residues, metal-binding, plasmid, secreted, virulence, immune system |
Biological source | Bacillus anthracis (anthrax,anthrax bacterium) |
Cellular location | Secreted, extracellular space: P13423 |
Total number of polymer chains | 2 |
Total formula weight | 32484.51 |
Authors | Lovell, S.,Williams, A.S.,Anbanandam, A.,El-Chami, R.,Bann, J.G. (deposition date: 2009-08-12, release date: 2009-11-03, Last modification date: 2023-09-06) |
Primary citation | 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 Cited by 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: 19722284DOI: 10.1002/pro.238 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report