2W7Y

Structure of a Streptococcus pneumoniae solute-binding protein in complex with the blood group A-trisaccharide.

2W7Y の概要

• エントリーDOI: 10.2210/pdb2w7y/pdb
• 分子名称: PROBABLE SUGAR ABC TRANSPORTER, SUGAR-BINDING PROTEIN, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: sugar-binding protein, solute-binding protein, streptococcus pneumoniae, blood group antigen, carbohydrate transport, sugar binding protein
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95652.76

構造登録者

Higgins, M.A.,Abbott, D.W.,Boulanger, M.J.,Boraston, A.B. (登録日: 2009-01-06, 公開日: 2009-03-10, 最終更新日: 2024-10-16)

主引用文献

Higgins, M.A.,Abbott, D.W.,Boulanger, M.J.,Boraston, A.B.
Blood-Group Antigen Recognition by a Solute-Binding Protein from a Serotype 3 Strain of Streptococcus Pneumoniae.
J.Mol.Biol., 388:299-, 2009

PubMed Abstract: Streptococcus pneumoniae is a common bacterial pathogen that is well known for its ability to cause acute respiratory disease (pneumonia), ear infections, and other serious illnesses. This Gram-positive bacterium relies on its carbohydrate-metabolizing capabilities for full virulence in its host; however, the range of glycan targets that it can attack is presently not fully appreciated. S. pneumoniae is known to have a fucose utilization operon that in the TIGR4 strain plays a role in its virulence. Here we identify a second type of fucose utilization operon that is present in a subset of S. pneumoniae strains, including the serotype 3 strain SP3-BS71. This operon contains a transporter with a solute-binding protein, FcsSBP (fucose solute-binding protein), that interacts tightly (Ka approximately 1 x 10(6) M(-1)) and specifically with soluble A- and B-antigen trisaccharides but displays no selectivity between these two sugars. The structure of the FcsSBP in complex with the A-trisaccharide antigen, determined to 2.35 A, reveals its mode of binding to the reducing end of this sugar, thus highlighting this protein's requirement for soluble blood group antigen ligands. Overall, this report exposes a heretofore unknown capability of certain S. pneumoniae strains to transport and potentially metabolize the histo-blood group antigen carbohydrates of its host.

PubMed: 19285508
DOI: 10.1016/J.JMB.2009.03.012

実験手法

X-RAY DIFFRACTION (2.35 Å)