PDBsum entry 6jlc

Toxin

PDB id: 6jlc

Contents

Protein chain

222 a.a.

Ligands

ACT

Waters ×171

PDB id:

6jlc

Name:

Toxin

Title:

Structure determination of camp factor of mobiluncus curtisii and insight into structural dynamics

Structure:

Camp factor. Chain: a. Engineered: yes

Source:

Mobiluncus curtisii (strain atcc 43063 / dsm 2711 / v125). Falcivibrio vaginalis. Organism_taxid: 548479. Strain: atcc 43063 / dsm 2711 / v125. Gene: hmpref0573_10472. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.85Å R-factor: 0.197 R-free: 0.229

Authors:

T.C.Jin,W.H.Zeng

Key ref:

W.Zeng et al. (2020). Structure determination of CAMP factor of Mobiluncus curtisii and insights into structural dynamics. Int J Biol Macromol, 150, 1027-1036. PubMed id: 31739050 DOI: 10.1016/j.ijbiomac.2019.10.107

Date:

04-Mar-19 Release date: 04-Dec-19

Protein chain

D6ZJ92  (D6ZJ92_MOBCV) -  cAMP factor from Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125)

Seq: 350 a.a.

Struc: 222 a.a.

DOI no: 10.1016/j.ijbiomac.2019.10.107

Int J Biol Macromol 150:1027-1036 (2020)

PubMed id: 31739050

Structure determination of CAMP factor of Mobiluncus curtisii and insights into structural dynamics.

W.Zeng, H.Ma, W.Fan, Y.Yang, C.Zhang, J.Arnaud Kombe Kombe, X.Fan, Y.Zhang, Z.Dong, Z.Shen, Y.Zhou, M.Yang, T.Jin.

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.