View source for 6jlc


==Structure determination of CAMP factor of Mobiluncus curtisii and insight into structural dynamics==
<StructureSection load='6jlc' size='340' side='right'caption='[[6jlc]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jlc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mobiluncus_curtisii_ATCC_43063 Mobiluncus curtisii ATCC 43063]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JLC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.847&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jlc OCA], [https://pdbe.org/6jlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jlc RCSB], [https://www.ebi.ac.uk/pdbsum/6jlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jlc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D6ZJ92_MOBCV D6ZJ92_MOBCV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 &gt;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 A 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.

Structure determination of CAMP factor of Mobiluncus curtisii and insights into structural dynamics.,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 Int J Biol Macromol. 2019 Nov 15. pii: S0141-8130(19)37284-8. doi:, 10.1016/j.ijbiomac.2019.10.107. PMID:31739050<ref>PMID:31739050</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jlc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mobiluncus curtisii ATCC 43063]]
[[Category: Jin TC]]
[[Category: Zeng WH]]