5DCL

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

Summary for 5DCL

• Entry DOI: 10.2210/pdb5dcl/pdb
• Descriptor: PhoB family transcriptional regulator, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: antimicrobial peptide, lantibiotic, nisin, resistance, regulation, two component system, signaling protein
• Biological source: Streptococcus agalactiae
• Total number of polymer chains: 2
• Total formula weight: 57934.41

Authors

Khosa, S.,Kleinschrodt, D.,Hoeppner, A.,Smits, S.H. (deposition date: 2015-08-24, release date: 2016-03-16, Last modification date: 2024-05-08)

Primary citation

Khosa, S.,Hoeppner, A.,Gohlke, H.,Schmitt, L.,Smits, S.H.
Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.
Plos One, 11:e0149903-e0149903, 2016

PubMed Abstract: 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.

PubMed: 26930060
DOI: 10.1371/journal.pone.0149903

Experimental method

X-RAY DIFFRACTION (1.41 Å)