View source for 4kdp


==TcaR-ssDNA complex crystal structure reveals the novel ssDNA binding mechanism of the MarR family proteins==
<StructureSection load='4kdp' size='340' side='right'caption='[[4kdp]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kdp]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis_ATCC_12228 Staphylococcus epidermidis ATCC 12228]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KDP 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]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4kdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kdp OCA], [https://pdbe.org/4kdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kdp RCSB], [https://www.ebi.ac.uk/pdbsum/4kdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kdp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2VJZ8_STAES A0A0H2VJZ8_STAES] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The teicoplanin-associated locus regulator (TcaR) regulates gene expression of proteins on the intercellular adhesion (ica) locus involved in staphylococci poly-N-acetylglucosamine biosynthesis. The absence of TcaR increases poly-N-acetylglucosamine production and promotes biofilm formation. Until recently, the mechanism of multiple antibiotic resistance regulator family protein members, such as TcaR, was restricted to binding double-stranded DNA. However, we recently found that TcaR strongly interacts with single-stranded DNA, which is a new role for this family of proteins. In this study, we report Staphylococcus epidermidis TcaR-single-stranded DNA complex structures. Our model suggests that TcaR and single-stranded DNA form a 61-symmetry polymer composed of TcaR dimers with single-stranded DNA that wraps outside the polymer and 12 nt per TcaR dimer. Single-stranded DNA binding to TcaR involves a large conformational change at the DNA binding lobe. Several point mutations involving the single-stranded DNA binding surface validate interactions between single-stranded DNA and TcaR. Our results extend the novel role of multiple antibiotic resistance regulator family proteins in staphylococci.

TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins.,Chang YM, Ho CH, Chen CK, Maestre-Reyna M, Chang-Chien MW, Wang AH Nucleic Acids Res. 2014 Feb 14. PMID:24531929<ref>PMID:24531929</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kdp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus epidermidis ATCC 12228]]
[[Category: Chang YM]]
[[Category: Chen CK-M]]
[[Category: Wang AH-J]]