High-resolution structures of the D-alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo- and holo-forms.
FEBS Lett
; 589(18): 2283-9, 2015 Aug 19.
Article
em En
| MEDLINE
| ID: mdl-26193422
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Apoproteínas
/
Bacillus subtilis
/
Proteínas de Bactérias
/
Proteínas de Transporte
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Alemanha