View source for 5dcl


==Structure of a lantibiotic response regulator: N terminal domain of the nisin resistance regulator NsrR==
<StructureSection load='5dcl' size='340' side='right'caption='[[5dcl]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dcl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5DCL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.41&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcl OCA], [https://pdbe.org/5dcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dcl RCSB], [https://www.ebi.ac.uk/pdbsum/5dcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dcl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/X5JZS1_STRAG X5JZS1_STRAG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dcl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus agalactiae]]
[[Category: Hoeppner A]]
[[Category: Khosa S]]
[[Category: Kleinschrodt D]]
[[Category: Smits SH]]