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5x5j

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Current revision (10:17, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5x5j' size='340' side='right'caption='[[5x5j]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='5x5j' size='340' side='right'caption='[[5x5j]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x5j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X5J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X5J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x5j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X5J FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x5l|5x5l]]</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">X-ray diffraction, [[Resolution|Resolution]] 1.401&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x5j OCA], [http://pdbe.org/5x5j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x5j RCSB], [http://www.ebi.ac.uk/pdbsum/5x5j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x5j ProSAT]</span></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=5x5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x5j OCA], [https://pdbe.org/5x5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x5j RCSB], [https://www.ebi.ac.uk/pdbsum/5x5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x5j 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/Q6TA00_ACIBA Q6TA00_ACIBA]
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AdeR-AdeS is a two-component regulatory system, which controls expression of the adeABC efflux pump involved in Acinetobacter baumannii multidrug resistance. AdeR is a response regulator consisting of an N-terminal receiver domain and a C-terminal DNA-binding-domain. AdeR binds to a direct-repeat DNA in the intercistronic region between adeR and adeABC. We demonstrate a markedly high affinity binding between unphosphorylated AdeR and DNA with a dissociation constant of 20 nM. In addition, we provide a 2.75 A crystal structure of AdeR DNA-binding-domain complexed with the intercistronic DNA. This structure shows that the alpha3 and beta hairpin formed by beta5-beta6 interacts with the major and minor groove of the DNA, which in turn leads to the introduction of a bend. The AdeR receiver domain structure revealed a dimerization motif mediated by a gearwheel-like structure involving the D108F109-R122 motif through cation pi stack interaction. The structure of AdeR receiver domain bound with magnesium indicated a conserved Glu19Asp20-Asp63 magnesium-binding motif, and revealed that the potential phosphorylation site Asp63OD1 forms a hydrogen bond with Lys112. We thus dissected the mechanism of how AdeR recognizes the intercistronic DNA, which leads to a diverse mode of response regulation. Unlocking the AdeRS mechanism provides ways to circumvent A. baumannii antibiotic resistance.
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Mechanistic insight into how multidrug resistant Acinetobacter baumannii response regulator AdeR recognizes an intercistronic region.,Wen Y, Ouyang Z, Yu Y, Zhou X, Pei Y, Devreese B, Higgins PG, Zheng F Nucleic Acids Res. 2017 Sep 19;45(16):9773-9787. doi: 10.1093/nar/gkx624. PMID:28934482<ref>PMID:28934482</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 5x5j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aciba]]
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[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Wen, Y]]
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[[Category: Wen Y]]
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[[Category: Ader]]
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[[Category: Bacterial signaling transduction]]
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[[Category: Dna binding protein]]
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[[Category: Response regulator]]
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[[Category: Two-component regulatory system]]
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Current revision

Crystal structure of response regulator AdeR receiver domain

PDB ID 5x5j

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OCA

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