3w9s
From Proteopedia
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| - | + | ==Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA== | |
| - | + | <StructureSection load='3w9s' size='340' side='right' caption='[[3w9s]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3w9s]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W9S FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KP1_1760 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=484021 Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w9s RCSB], [http://www.ebi.ac.uk/pdbsum/3w9s PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Klebsiella pneumoniae subsp. pneumoniae ntuh-k2044]] | [[Category: Klebsiella pneumoniae subsp. pneumoniae ntuh-k2044]] | ||
| - | [[Category: Chen, C | + | [[Category: Chen, C]] |
| - | [[Category: Luo, S | + | [[Category: Luo, S]] |
[[Category: Alpha and beta protein]] | [[Category: Alpha and beta protein]] | ||
[[Category: Polymyxin b resistant protein some]] | [[Category: Polymyxin b resistant protein some]] | ||
Revision as of 08:57, 20 January 2015
Crystal Structure Analysis of the N-terminal Receiver domain of Response Regulator PmrA
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