High‐resolution structures of the d‐alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo‐ and holo‐forms

d‐Alanylation of lipoteichoic acids plays an important role in modulating the properties of Gram‐positive bacteria cell walls. The d‐alanyl carrier protein DltC from Bacillus subtilis has been solved in apo‐ and two cofactor‐modified holo‐forms, whereby the entire phosphopantetheine moiety is defined in one. The atomic resolution of the apo‐structure allows delineation of alternative conformations within the hydrophobic core of the 78 residue four helix bundle. In contrast to previous reports for a peptidyl carrier protein from a non‐ribosomal peptide synthetase, no obvious structural differences between apo‐ and holo‐DltC forms are observed. Solution NMR spectroscopy confirms these findings and demonstrates in addition that the two forms exhibit similar backbone dynamics on the ps–ns and ms timescales.

• Publication year

  2015

• Venue

  FEBS Letters

• Publication date

  2015-08-19

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.febslet.2015.07.008PMID 26193422
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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