View source for 4oqq


==Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis==
<StructureSection load='4oqq' size='340' side='right'caption='[[4oqq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4oqq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OQQ 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</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=4oqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqq OCA], [https://pdbe.org/4oqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oqq RCSB], [https://www.ebi.ac.uk/pdbsum/4oqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEOR_BACSU DEOR_BACSU] Negative regulator of the dra-nupC-pdp operon. DeoR binds cooperatively to the operator DNA, which consists of a palindrome and a direct repeat sequence located 3' to the palindrome.
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== Publication Abstract from PubMed ==
Deoxyribonucleoside regulator DeoR from Bacillus subtilis negatively regulates expression of enzymes involved in the catabolism of deoxyribonucleosides and deoxyribose. The DeoR protein is homologous to the sorbitol operon regulator family of metabolic regulators and comprises an N-terminal DNA-binding domain and a C-terminal effector-binding domain. We have determined the crystal structure of the effector-binding domain of DeoR (C-DeoR) in free form and in covalent complex with its effector deoxyribose-5-phosphate (dR5P). This is the first case of a covalently attached effector molecule captured in the structure of a bacterial transcriptional regulator. The dR5P molecule is attached through a Schiff base linkage to residue Lys141. The crucial role of Lys141 in effector binding was confirmed by mutational analysis and mass spectrometry of Schiff base adducts formed in solution. Structural analyses of the free and effector-bound C-DeoR structures provided a structural explanation for mechanism of DeoR function as a molecular switch. This article is protected by copyright. All rights reserved.

Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis.,Skerlova J, Fabry M, Hubalek M, Otwinowski Z, Rezacova P FEBS J. 2014 May 23. doi: 10.1111/febs.12856. PMID:24863636<ref>PMID:24863636</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4oqq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Rezacova P]]
[[Category: Skerlova J]]