6JLC
Structure determination of CAMP factor of Mobiluncus curtisii and insight into structural dynamics
Summary for 6JLC
| Entry DOI | 10.2210/pdb6jlc/pdb |
| Descriptor | CAMP factor, ACETATE ION (3 entities in total) |
| Functional Keywords | bacterial vaginosis, mobiluncus curtisii, toxin, pore-forming-factor, hemolytic reaction. |
| Biological source | Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio vaginalis) |
| Total number of polymer chains | 1 |
| Total formula weight | 25628.98 |
| Authors | Jin, T.C.,Zeng, W.H. (deposition date: 2019-03-04, release date: 2019-12-04, Last modification date: 2023-11-22) |
| Primary citation | Zeng, W.,Ma, H.,Fan, W.,Yang, Y.,Zhang, C.,Arnaud Kombe Kombe, J.,Fan, X.,Zhang, Y.,Dong, Z.,Shen, Z.,Zhou, Y.,Yang, M.,Jin, T. Structure determination of CAMP factor of Mobiluncus curtisii and insights into structural dynamics. Int.J.Biol.Macromol., 150:1027-1036, 2020 Cited by PubMed Abstract: Bacterial vaginosis (BV) is a common type of vaginal inflammation caused by a proliferation of pathogenic bacteria, among which Mobiluncus curtisii. In our previous studies on M. curtisii genome, we identified the presence of a genomic fragment encoding a 25 kDa pore-forming toxin, the CAMP factor, which is known to be involved in the synergistic lysis of erythrocytes namely CAMP reaction. However, whether this hypothetical gene product has hemolytic activity is unknown. Moreover, its relative structure and function are not yet solved. Here we found that the M. curtisii CAMP factor is a monomer at pH 4.4 and oligomer at pH > 4.6. Hemolysis assays showed that M. curtisii CAMP factor could lyse sheep red blood cells efficiently in pH 5.4-7.4. Negative staining electron microscope analysis of the CAMP factor revealed ring-like structures at pH above 4.6. Additionally, the crystal structure of M. curtisii CAMP factor, determineded at 1.85 Å resolution, reveals a 5 + 3 helix motif. Further functional analysis suggested that the structural rearrangement of the N-terminal domain might be required for protein function. In conclusion, this structure-function relationship study of CAMP factor provides a new perspective of the M. curtisii role in BV development. PubMed: 31739050DOI: 10.1016/j.ijbiomac.2019.10.107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.847 Å) |
Structure validation
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