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5dcm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a lantibiotic response regulator: C-terminal domain of the nisin resistance regulator NsrR== | |
| + | <StructureSection load='5dcm' size='340' side='right'caption='[[5dcm]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dcm]] 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=5DCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DCM 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]] 1.6Å</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=5dcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcm OCA], [https://pdbe.org/5dcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dcm RCSB], [https://www.ebi.ac.uk/pdbsum/5dcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dcm 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5dcm" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus agalactiae]] | ||
| + | [[Category: Hoeppner A]] | ||
| + | [[Category: Khosa S]] | ||
| + | [[Category: Kleinschrodt D]] | ||
| + | [[Category: Smits SHJ]] | ||
Current revision
Structure of a lantibiotic response regulator: C-terminal domain of the nisin resistance regulator NsrR
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