1PP0
volvatoxin A2 in monoclinic crystal
Summary for 1PP0
Entry DOI | 10.2210/pdb1pp0/pdb |
Related | 1PP6 1VCY 1VGF |
Descriptor | volvatoxin A2, ACETIC ACID (3 entities in total) |
Functional Keywords | volvatoxin a2, ingot crystal form, toxin |
Biological source | Volvariella volvacea |
Total number of polymer chains | 4 |
Total formula weight | 90208.52 |
Authors | Lin, S.-C.,Lo, Y.-C.,Lin, J.-Y.,Liaw, Y.-C. (deposition date: 2003-06-16, release date: 2004-08-24, Last modification date: 2023-10-25) |
Primary citation | Lin, S.-C.,Lo, Y.-C.,Lin, J.-Y.,Liaw, Y.-C. Crystal structures and electron micrographs of fungal volvatoxin A2 J.Mol.Biol., 343:477-491, 2004 Cited by PubMed Abstract: Membrane adhesion and insertion of protein are essential to all organisms, but the underlying mechanisms remain largely unknown. Membrane pore-forming toxins (PFTs) are potential model systems for studying these mechanisms. We have determined the crystal structures of volvatoxin A2 (VVA2), a fungal PFT from Volvariella volvacea, using Br-multiple-wavelength anomalous diffraction (MAD). The VVA2 structures obtained at pH 4.6, pH 5.5 and pH 6.5 were refined to resolutions of 1.42 A, 2.6 A and 3.2 A, respectively. The structures reveal that the VVA2 monomer contains a single alpha/beta domain. Most of the VVA2 surface is occupied by its oligomerization motif and two putative heparin-binding motifs. Residues Ala91 to Ala101 display several conformations at different pH values, which might be under the control of His87. We also found that the shape of one putative heparin-binding motif in VVA2 appears similar to those found in fibroblast growth factors, and the other one displays a linear polypeptide. Our results suggest several possible intermediates of protein assembly in solution and protein adhering to cell membranes before conformational changes. The electron micrographs of VVA2 molecules in solution, at a protein concentration of 1 microg ml(-1), show that they can assemble into filament-like or braid-like oligomers in a pH-dependent way. In addition, the arc-shaped VVA2 structure obtained at pH 6.5 suggests that VVA2 could form a two-layered helical oligomer with 18 subunits per turn. The structures presented here could be used to elucidate the pore-formation mechanisms of VVA2 and its structural neighbors, Cyt toxins from Bacillus thuringiensis. PubMed: 15451675DOI: 10.1016/j.jmb.2004.08.045 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.42 Å) |
Structure validation
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