8WL7

X-ray structure of Enterobacter cloacae allose-binding protein in complex with D-allose

Summary for 8WL7

• Entry DOI: 10.2210/pdb8wl7/pdb
• Related: 8WL5
• Descriptor: Allose ABC transporter, beta-D-allopyranose (3 entities in total)
• Functional Keywords: allose-binding protein, sugar binding protein
• Biological source: Enterobacter cloacae
• Total number of polymer chains: 1
• Total formula weight: 33001.72

Authors

Kamitori, S. (deposition date: 2023-09-29, release date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.74 Å)