3HIA

Crystal structure of the choline binding domain of Spr1274 in Streptococcus pneumoniae

Summary for 3HIA

• Entry DOI: 10.2210/pdb3hia/pdb
• Descriptor: Choline binding protein, PHOSPHOCHOLINE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: beta hairpin, choline-binding protein
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 3
• Total formula weight: 34057.75

Authors

Zhang, Z.-Y.,Li, W.-Z.,Jiang, Y.-L.,Bao, R.,Zhou, C.-Z.,Chen, Y.-X. (deposition date: 2009-05-19, release date: 2009-08-04, Last modification date: 2025-05-07)

Primary citation

Zhang, Z.,Li, W.,Frolet, C.,Bao, R.,di Guilmi, A.M.,Vernet, T.,Chen, Y.
Structure of the choline-binding domain of Spr1274 in Streptococcus pneumoniae.
Acta Crystallogr.,Sect.F, 65:757-761, 2009

PubMed 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.

PubMed: 19652332
DOI: 10.1107/S1744309109025329

Experimental method

X-RAY DIFFRACTION (2.38 Å)