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3w9s

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'''Unreleased structure'''
 
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The entry 3w9s is ON HOLD
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==Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA==
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<StructureSection load='3w9s' size='340' side='right'caption='[[3w9s]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3w9s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_NTUH-K2044 Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W9S 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">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3w9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9s OCA], [https://pdbe.org/3w9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w9s RCSB], [https://www.ebi.ac.uk/pdbsum/3w9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w9s 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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In bacteria, the two-component system is the most prevalent for sensing and transducing environmental signals into the cell. The PmrA-PmrB two-component system, responsible for sensing external stimuli of high Fe(3+) and mild acidic conditions, can control the genes involved in lipopolysaccharide modification and polymyxin resistance in pathogens. In Klebsiella pneumoniae, the small basic connector protein PmrD protects phospho-PmrA and prolongs the expression of PmrA-activated genes. We previously determined the phospho-PmrA recognition mode of PmrD. However, how PmrA interacts with PmrD and prevents its dephosphorylation remains unknown. To address this question, we solved the x-ray crystal structure of the N-terminal receiver domain of BeF3(-)-activated PmrA (PmrAN) at 1.70 A. With this structure, we applied the data-driven docking method based on NMR chemical shift perturbation to generate the complex model of PmrD-PmrAN, which was further validated by site-directed spin labeling experiments. In the complex model, PmrD may act as a blockade to prevent phosphatase from contacting with the phosphorylation site on PmrA.
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Authors: Chen, C., Luo, S.
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Structural Basis of a Physical Blockage Mechanism for the Interaction of Response Regulator PmrA with Connector Protein PmrD from Klebsiella pneumoniae.,Luo SC, Lou YC, Rajasekaran M, Chang YW, Hsiao CD, Chen C J Biol Chem. 2013 Aug 30;288(35):25551-61. doi: 10.1074/jbc.M113.481978. Epub, 2013 Jul 16. PMID:23861396<ref>PMID:23861396</ref>
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Description: Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA
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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 3w9s" 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 subsp. pneumoniae NTUH-K2044]]
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[[Category: Large Structures]]
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[[Category: Chen C]]
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[[Category: Luo S]]

Current revision

Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA

PDB ID 3w9s

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