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PDBsum entry 6jlc
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References listed in PDB file
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Key reference
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Title
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Structure determination of camp factor of mobiluncus curtisii and insights into structural dynamics.
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Authors
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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.
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Ref.
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Int J Biol Macromol, 2020,
150,
1027-1036.
[DOI no: ]
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PubMed id
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Abstract
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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.
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