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

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 A resolution with three molecules in the asymmetric unit. It may provide a structural basis for functional analysis of choline-binding proteins.

SUBMITTER: Zhang Z

PROVIDER: S-EPMC2720326 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

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

Zhang Zhenyi Z Li Wenzhe W Frolet Cecile C Bao Rui R di Guilmi Anne Marie AM Vernet Thierry T Chen Yuxing Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20090721 Pt 8

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 A resolution with three molecules in the asymmetric unit. It may provide a structural basis for functional analysis of choline-binding proteins. ...[more]

PMID: 19652332

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