3MA0

Closed liganded crystal structure of xylose binding protein from Escherichia coli

3MA0 の概要

• エントリーDOI: 10.2210/pdb3ma0/pdb
• 関連するPDBエントリー: 3M9W 3M9X
• 分子名称: D-xylose-binding periplasmic protein, beta-D-xylopyranose (3 entities in total)
• 機能のキーワード: xylose binding protein, xylose, conformational changes, sugar binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P37387
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 102854.59

構造登録者

Sooriyaarachchi, S.,Ubhayasekera, W.,Mowbray, S.L. (登録日: 2010-03-23, 公開日: 2010-08-18, 最終更新日: 2023-11-01)

主引用文献

Sooriyaarachchi, S.,Ubhayasekera, W.,Park, C.,Mowbray, S.L.
Conformational changes and ligand recognition of Escherichia coli D-xylose binding protein revealed
J.Mol.Biol., 402:657-668, 2010

PubMed Abstract: ATP binding cassette transport systems account for most import of necessary nutrients in bacteria. The periplasmic binding component (or an equivalent membrane-anchored protein) is critical to recognizing cognate ligand and directing it to the appropriate membrane permease. Here we report the X-ray structures of D-xylose binding protein from Escherichia coli in ligand-free open form, ligand-bound open form, and ligand-bound closed form at 2.15 Å, 2.2 Å, and 2.2 Å resolutions, respectively. The ligand-bound open form is the first such structure to be reported at high resolution; the combination of the three different forms from the same protein furthermore gives unprecedented details concerning the conformational changes involved in binding protein function. As is typical of the structural family, the protein has two similar globular domains, which are connected by a three-stranded hinge region. The open liganded structure shows that xylose binds first to the C-terminal domain, with only very small conformational changes resulting. After a 34° closing motion, additional interactions are formed with the N-terminal domain; changes in this domain are larger and serve to make the structure more ordered near the ligand. An analysis of the interactions suggests why xylose is the preferred ligand. Furthermore, a comparison with the most closely related proteins in the structural family shows that the conformational changes are distinct in each type of binding protein, which may have implications for how the individual proteins act in concert with their respective membrane permeases.

PubMed: 20678502
DOI: 10.1016/j.jmb.2010.07.038

実験手法

X-RAY DIFFRACTION (2.2 Å)