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Media type:
E-Article
Title:
High‐resolution structures of the d‐alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo‐ and holo‐forms
Published in:
FEBS Letters, 589 (2015) 18, Seite 2283-2289
Language:
English
DOI:
10.1016/j.febslet.2015.07.008
ISSN:
1873-3468;
0014-5793
Origination:
Footnote:
Description:
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.