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5zuz

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Current revision (07:29, 1 May 2024) (edit) (undo)
 
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==Solution Structure of the DNA-Binding Domain of Rok==
==Solution Structure of the DNA-Binding Domain of Rok==
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<StructureSection load='5zuz' size='340' side='right'caption='[[5zuz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5zuz' size='340' side='right'caption='[[5zuz]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zuz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZUZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zuz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZUZ FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuz OCA], [http://pdbe.org/5zuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zuz RCSB], [http://www.ebi.ac.uk/pdbsum/5zuz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuz ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zuz OCA], [https://pdbe.org/5zuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zuz RCSB], [https://www.ebi.ac.uk/pdbsum/5zuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zuz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/ROK_BACSU ROK_BACSU] Repressor of comK, the master regulator of competence development (PubMed:11849533). Overexpression seems to be lethal (PubMed:11849533). Represses at least 20 genes that specify membrane-localized and secreted proteins, including some that encode products with antibiotic activity (PubMed:15743949). Binds to many AT-rich sites in the chromosome, many of which are known or thought to derive from horizontal gene transfer; helps keep mobile element ICEBs1 quiescent in the genome (PubMed:21085634). Binds to its own promoter and is thus probably autoregulatory (PubMed:21085634).<ref>PMID:11849533</ref> <ref>PMID:15743949</ref> <ref>PMID:21085634</ref>
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Bacterial xenogeneic silencers play important roles in bacterial evolution by recognizing and inhibiting expression from foreign genes acquired through horizontal gene transfer, thereby buffering against potential fitness consequences of their misregulated expression. Here, the detailed DNA binding properties of Rok, a xenogeneic silencer in Bacillus subtilis, was studied using protein binding microarray, and the solution structure of its C-terminal DNA binding domain was determined in complex with DNA. The C-terminal domain of Rok adopts a typical winged helix fold, with a novel DNA recognition mechanism different from other winged helix proteins or xenogeneic silencers. Rok binds the DNA minor groove by forming hydrogen bonds to bases through N154, T156 at the N-terminal of alpha3 helix and R174 of wing W1, assisted by four lysine residues interacting electrostatically with DNA backbone phosphate groups. These structural features endow Rok with preference towards DNA sequences harboring AACTA, TACTA, and flexible multiple TpA steps, while rigid A-tracts are disfavored. Correspondingly, the Bacillus genomes containing Rok are rich in A-tracts and show a dramatic underrepresentation of AACTA and TACTA, which are significantly enriched in Rok binding regions. These observations suggest that the xenogeneic silencing protein and its resident genome may have evolved cooperatively.
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How bacterial xenogeneic silencer rok distinguishes foreign from self DNA in its resident genome.,Duan B, Ding P, Hughes TR, Navarre WW, Liu J, Xia B Nucleic Acids Res. 2018 Sep 25. pii: 5106470. doi: 10.1093/nar/gky836. PMID:30252102<ref>PMID:30252102</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5zuz" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Duan, B]]
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[[Category: Duan B]]
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[[Category: Xia, B]]
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[[Category: Xia B]]
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[[Category: Dna binding protein]]
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[[Category: Winged helix]]
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[[Category: Xenogeneic silencer]]
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Current revision

Solution Structure of the DNA-Binding Domain of Rok

PDB ID 5zuz

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