4BPG

Crystal structure of Bacillus subtilis DltC

Summary for 4BPG

• Entry DOI: 10.2210/pdb4bpg/pdb
• Related: 4BPF 4BPH
• Descriptor: D-ALANINE--POLY(PHOSPHORIBITOL) LIGASE SUBUNIT 2 (2 entities in total)
• Functional Keywords: ligase, lipoteichoic acid, d-alanylation, peptidyl-carrier-protein, acyl-carrier-protein
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 2
• Total formula weight: 20334.44

Authors

Yonus, H.,Zimmermann, S.,Neumann, P.,Stubbs, M.T. (deposition date: 2013-05-26, release date: 2014-06-11, Last modification date: 2024-10-23)

Primary citation

Zimmermann, S.,Pfennig, S.,Neumann, P.,Yonus, H.,Weininger, U.,Kovermann, M.,Balbach, J.,Stubbs, M.T.
High-Resolution Structures of the D-Alanyl Carrier Protein (Dcp) Dltc from Bacillus Subtilis Reveal Equivalent Conformations of Apo- and Holo-Forms
FEBS Lett., 589:2283-, 2015

PubMed 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.

PubMed: 26193422
DOI: 10.1016/J.FEBSLET.2015.07.008

Experimental method

X-RAY DIFFRACTION (2.2 Å)