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5dcl

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'''Unreleased structure'''
 
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The entry 5dcl is ON HOLD until Paper Publication
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==Structure of a lantibiotic response regulator: N terminal domain of the nisin resistance regulator NsrR==
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<StructureSection load='5dcl' size='340' side='right' caption='[[5dcl]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5dcl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DCL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<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=5dcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcl OCA], [http://pdbe.org/5dcl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dcl RCSB], [http://www.ebi.ac.uk/pdbsum/5dcl PDBsum]</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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Lantibiotics are antimicrobial peptides produced by Gram-positive bacteria. Interestingly, several clinically relevant and human pathogenic strains are inherently resistant towards lantibiotics. The expression of the genes responsible for lantibiotic resistance is regulated by a specific two-component system consisting of a histidine kinase and a response regulator. Here, we focused on a response regulator involved in lantibiotic resistance, NsrR from Streptococcus agalactiae, and determined the crystal structures of its N-terminal receiver domain and C-terminal DNA-binding effector domain. The C-terminal domain exhibits a fold that classifies NsrR as a member of the OmpR/PhoB subfamily of regulators. Amino acids involved in phosphorylation, dimerization, and DNA-binding were identified and demonstrated to be conserved in lantibiotic resistance regulators. Finally, a model of the full-length NsrR in the active and inactive state provides insights into protein dimerization and DNA-binding.
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Authors: Khosa, S., Kleinschrodt, D., Hoeppner, A., Smits, S.H.
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Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.,Khosa S, Hoeppner A, Gohlke H, Schmitt L, Smits SH PLoS One. 2016 Mar 1;11(3):e0149903. doi: 10.1371/journal.pone.0149903., eCollection 2016. PMID:26930060<ref>PMID:26930060</ref>
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Description: Structure of a lantibiotic response regulator: N terminal domain of the nisin resistance regulator NsrR
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kleinschrodt, D]]
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<div class="pdbe-citations 5dcl" 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>
[[Category: Hoeppner, A]]
[[Category: Hoeppner, A]]
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[[Category: Smits, S.H]]
 
[[Category: Khosa, S]]
[[Category: Khosa, S]]
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[[Category: Kleinschrodt, D]]
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[[Category: Smits, S H]]
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[[Category: Antimicrobial peptide]]
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[[Category: Lantibiotic]]
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[[Category: Nisin]]
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[[Category: Regulation]]
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[[Category: Resistance]]
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[[Category: Signaling protein]]
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[[Category: Two component system]]

Revision as of 03:47, 11 May 2016

Structure of a lantibiotic response regulator: N terminal domain of the nisin resistance regulator NsrR

5dcl, resolution 1.41Å

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