title: 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.
authors: Protein Research Institute, Tongji University, Shanghai 200092, People's Republic of China.
authors: Zhenyi
authors: Z
authors: Zhang
authors: Wenzhe
authors: W
authors: Li
authors: Cecile
authors: C
authors: Frolet
authors: Rui
authors: R
authors: Bao
authors: Anne Marie
authors: AM
authors: di Guilmi
authors: Thierry
authors: T
authors: Vernet
authors: Yuxing
authors: Y
authors: Chen
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002794:Choline / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013296:Streptococcus pneumoniae / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D002794:Choline