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5dcm
From Proteopedia
(Difference between revisions)
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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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DCM FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dcl|5dcl]]</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=5dcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcm OCA], [http://pdbe.org/5dcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dcm RCSB], [http://www.ebi.ac.uk/pdbsum/5dcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dcm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5dcm" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hoeppner, A]] | [[Category: Hoeppner, A]] | ||
[[Category: Khosa, S]] | [[Category: Khosa, S]] | ||
| + | [[Category: Kleinschrodt, D]] | ||
| + | [[Category: Smits, S H.J]] | ||
| + | [[Category: Antimicrobial peptide]] | ||
| + | [[Category: Lantibiotic]] | ||
| + | [[Category: Nisin]] | ||
| + | [[Category: Resistance/regulation]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Two component system]] | ||
Revision as of 02:21, 13 July 2016
Structure of a lantibiotic response regulator: C-terminal domain of the nisin resistance regulator NsrR
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