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Expression, purification, crystallization and preliminary X-ray analysis of the D-alanyl carrier protein DltC from Staphylococcus epidermidis.

Authors :
Huang CH
Kao CH
Yang CS
Chang CH
Chen SC
Kuan SM
Su YC
Huang YH
Chang MC
Chen Y
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2012 Jul 01; Vol. 68 (Pt 7), pp. 810-2. Date of Electronic Publication: 2012 Jun 28.
Publication Year :
2012

Abstract

The D-alanyl lipoteichoic acids (D-alanyl LTAs) present in the cell walls of Gram-positive bacteria play crucial roles in autolysis, cation homeostasis and biofilm formation. The alanylation of LTAs requires the D-alanyl carrier protein DltC to transfer D-Ala onto a membrane-associated LTA. Here, DltC from Staphylococcus epidermidis (SeDltC) was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.83 Å and belonged to space group P2, with unit-cell parameters a = 66.26, b = 53.28, c = 88.05 Å, β = 98.22°. The results give a preliminary crystallographic analysis of SeDltC and shed light on the functional role of DltC in the alanylation of LTAs.

Details

Language :
English
ISSN :
1744-3091
Volume :
68
Issue :
Pt 7
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
22750871
Full Text :
https://doi.org/10.1107/S1744309112021720