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Structure of the choline-binding domain of Spr1274 in Streptococcus pneumoniae.

Authors :
Zhang, Zhenyi
Li, Wenzhe
Frolet, Cecile
Bao, Rui
Di Guilmi, Anne-Marie
Vernet, Thierry
Chen, Yuxing
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Aug2009, Vol. 65 Issue 8, p757-761. 5p.
Publication Year :
2009

Abstract

Spr1274 is a putative choline-binding protein that is bound to the cell wall of Streptococcus pneumoniae through noncovalent interactions with the choline moieties of teichoic and lipoteichoic acids. Its function is still unknown. The crystal structure of the choline-binding domain of Spr1274 (residues 44-129) was solved at 2.38 Å resolution with three molecules in the asymmetric unit. It may provide a structural basis for functional analysis of choline-binding proteins. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
65
Issue :
8
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
110812259
Full Text :
https://doi.org/10.1107/S1744309109025329