2mlk

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'''Unreleased structure'''
 
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The entry 2mlk is ON HOLD until Paper Publication
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==Three-dimensional structure of the C-terminal DNA-binding domain of RstA protein from Klebsiella pneumoniae==
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<StructureSection load='2mlk' size='340' side='right'caption='[[2mlk]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mlk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLK FirstGlance]. <br>
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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=2mlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlk OCA], [https://pdbe.org/2mlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlk RCSB], [https://www.ebi.ac.uk/pdbsum/2mlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlk ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The RstA/RstB system is a bacterial two-component regulatory system consisting of the membrane sensor, RstB and its cognate response regulator (RR) RstA. The RstA of Klebsiella pneumoniae (kpRstA) consists of an N-terminal receiver domain (RD, residues 1-119) and a C-terminal DNA-binding domain (DBD, residues 130-236). Phosphorylation of kpRstA induces dimerization, which allows two kpRstA DBDs to bind to a tandem repeat, called the RstA box, and regulate the expression of downstream genes. Here we report the solution and crystal structures of the free kpRstA RD, DBD and DBD/RstA box DNA complex. The structure of the kpRstA DBD/RstA box complex suggests that the two protomers interact with the RstA box in an asymmetric fashion. Equilibrium binding studies further reveal that the two protomers within the kpRstA dimer bind to the RstA box in a sequential manner. Taken together, our results suggest a binding model where dimerization of the kpRstA RDs provides the platform to allow the first kpRstA DBD protomer to anchor protein-DNA interaction, whereas the second protomer plays a key role in ensuring correct recognition of the RstA box.
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Authors: Fang, P., Chen, S., Cheng, Y., Chang, C., Yu, T., Huang, T.
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Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element.,Li YC, Chang CK, Chang CF, Cheng YH, Fang PJ, Yu T, Chen SC, Li YC, Hsiao CD, Huang TH Nucleic Acids Res. 2014 Jul 2. pii: gku572. PMID:24990372<ref>PMID:24990372</ref>
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Description: Three-dimensional structure of the C-terminal DNA-binding domain of RstA protein from Klebsiella pneumoniae
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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 2mlk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Klebsiella pneumoniae]]
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[[Category: Large Structures]]
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[[Category: Chang C]]
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[[Category: Chen S]]
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[[Category: Cheng Y]]
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[[Category: Fang P]]
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[[Category: Huang T]]
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[[Category: Yu T]]

Current revision

Three-dimensional structure of the C-terminal DNA-binding domain of RstA protein from Klebsiella pneumoniae

PDB ID 2mlk

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