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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt 8):757-61. doi: 10.1107/S1744309109025329. Epub 2009 Jul 21.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Choline / metabolism*
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Open Reading Frames
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Streptococcus pneumoniae / metabolism*

Substances

  • Bacterial Proteins
  • Choline

Associated data

  • PDB/3HIA
  • PDB/R3HIASF
  • PDB/SPR1274