View source for 5vfx


==Structure of an accessory protein of the pCW3 relaxosome in complex with the origin of transfer (oriT) DNA==
<StructureSection load='5vfx' size='340' side='right'caption='[[5vfx]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vfx]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VFX 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]] 2.81&#8491;</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=5vfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vfx OCA], [https://pdbe.org/5vfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vfx RCSB], [https://www.ebi.ac.uk/pdbsum/5vfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vfx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1PLI2_CLOPF Q1PLI2_CLOPF] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Conjugation is fundamental for the acquisition of new genetic traits and the development of antibiotic resistance in pathogenic organisms. Here, we show that a hypothetical Clostridium perfringens protein, TcpK, which is encoded by the tetracycline resistance plasmid pCW3, is essential for efficient conjugative DNA transfer. Our studies reveal that TcpK is a member of the winged helix-turn-helix (wHTH) transcription factor superfamily and that it forms a dimer in solution. Furthermore, TcpK specifically binds to a nine-nucleotide sequence that is present as tandem repeats within the pCW3 origin of transfer (oriT). The X-ray crystal structure of the TcpK-TcpK box complex reveals a binding mode centered on and around the beta-wing, which is different from what has been previously shown for other wHTH proteins. Structure-guided mutagenesis experiments validate the specific interaction between TcpK and the DNA molecule. Additional studies highlight that the TcpK dimer is important for specific DNA binding.

Crystal structure of TcpK in complex with oriT DNA of the antibiotic resistance plasmid pCW3.,Traore DAK, Wisniewski JA, Flanigan SF, Conroy PJ, Panjikar S, Mok YF, Lao C, Griffin MDW, Adams V, Rood JI, Whisstock JC Nat Commun. 2018 Sep 13;9(1):3732. doi: 10.1038/s41467-018-06096-2. PMID:30213934<ref>PMID:30213934</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vfx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Adams V]]
[[Category: Conroy PJ]]
[[Category: Flanigan SF]]
[[Category: Griffin MDW]]
[[Category: Lao C]]
[[Category: Mok Y-F]]
[[Category: Panjikar S]]
[[Category: Rood JI]]
[[Category: Traore DAK]]
[[Category: Whisstock JC]]
[[Category: Wisniewski JA]]