5XS8

Crystal structure of solute-binding protein complexed with unsaturated chondroitin disaccharide with two sulfate groups at C-4 and C-6 positions of GalNAc

5XS8 の概要

• エントリーDOI: 10.2210/pdb5xs8/pdb
• 分子名称: Extracellular solute-binding protein family 1, 4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid-(1-3)-2-acetamido-2-deoxy-4,6-di-O-sulfo-beta-D-galactopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: glycosaminoglycan, abc transporter, solute-binding protein, sugar binding protein
• 由来する生物種: Streptobacillus moniliformis DSM 12112
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 232446.98

構造登録者

Oiki, S.,Kamochi, R.,Mikami, B.,Murata, K.,Hashimoto, W. (登録日: 2017-06-12, 公開日: 2018-01-17, 最終更新日: 2023-11-22)

主引用文献

Oiki, S.,Kamochi, R.,Mikami, B.,Murata, K.,Hashimoto, W.
Alternative substrate-bound conformation of bacterial solute-binding protein involved in the import of mammalian host glycosaminoglycans.
Sci Rep, 7:17005-17005, 2017

PubMed Abstract: Glycosaminoglycans (GAGs), constituted by repeating uronate and amino sugar units, are major components of mammalian extracellular matrices. Some indigenous and pathogenic bacteria target GAGs for colonization to and/or infection of host mammalian cells. In Gram-negative pathogenic Streptobacillus moniliformis, the solute-binding protein (Smon0123)-dependent ATP-binding cassette (ABC) transporter incorporates unsaturated GAG disaccharides into the cytoplasm after depolymerization by polysaccharide lyase. Smon0123, composed of N and C domains, adopts either a substrate-free open or a substrate-bound closed form by approaching two domains at 47° in comparison with the open form. Here we show an alternative 39°-closed conformation of Smon0123 bound to unsaturated chondroitin disaccharide sulfated at the C-4 and C-6 positions of N-acetyl-d-galactosamine residue (CΔ4S6S). In CΔ4S6S-bound Smon0123, Arg204 and Lys210 around the two sulfate groups were located at different positions from those at other substrate-bound 47°-closed conformations. Therefore, the two sulfate groups in CΔ4S6S shifted substrate-binding residue arrangements, causing dynamic conformational change. Smon0123 showed less affinity with CΔ4S6S than with non-sulfated and monosulfated substrates. ATPase activity of the Smon0123-dependent ABC transporter in the presence of CΔ4S6S was lower than that in the presence of other unsaturated chondroitin disaccharides, suggesting that CΔ4S6S-bound Smon0123 was unpreferable for docking with the ABC transporter.

PubMed: 29208901
DOI: 10.1038/s41598-017-16801-8

実験手法

X-RAY DIFFRACTION (1.952 Å)