8WL5

X-ray structure of Enterobacter cloacae allose-binding protein in free form

8WL5 の概要

• エントリーDOI: 10.2210/pdb8wl5/pdb
• 分子名称: Allose ABC transporter, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: allose-binding protein, sugar binding protein
• 由来する生物種: Enterobacter cloacae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32883.63

構造登録者

Kamitori, S. (登録日: 2023-09-29, 公開日: 2023-10-25)

主引用文献

Kamitori, S.
X-ray structures of Enterobacter cloacae allose-binding protein in complexes with monosaccharides demonstrate its unique recognition mechanism for high affinity to allose.
Biochem.Biophys.Res.Commun., 682:187-192, 2023

PubMed Abstract: d-Allose is an aldohexose of the C3-epimer of d-glucose, existing in very small amounts in nature, called a rare sugar. The operon responsible for d-allose metabolism, the allose operon, was found in several bacteria, which consists of seven genes: alsR, alsB, alsA, alsC, alsE, alsK, and rpiB. To understand the biological implication of the allose operon utilizing a rare sugar of d-allose as a carbon source, it is important to clarify whether the allose operon functions specifically for d-allose or also functions for other ligands. It was proposed that the allose operon can function for d-ribose, which is essential as a component of nucleotides and abundant in nature. Allose-binding protein, AlsB, coded in the allose operon, is thought to capture a ligand outside the cell, and is expected to show high affinity for the specific ligand. X-ray structure determinations of Enterobacter cloacae AlsB (EtcAlsB) in ligand-free form, and in complexes with d-allose, d-ribose, and d-allulose, and measurements of the thermal parameters of the complex formation using an isothermal titration calorimeter were performed. The results demonstrated that EtcAlsB has a unique recognition mechanism for high affinity to d-allose by changing its conformation from an open to a closed form depending on d-allose-binding, and that the binding of d-ribose to EtcAlsB could not induce a completely closed form but an intermediate form, explaining the low affinity for d-ribose.

PubMed: 37820454
DOI: 10.1016/j.bbrc.2023.10.016

実験手法

X-RAY DIFFRACTION (1.87 Å)