5YQW

Structure and function of a novel periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria

5YQW の概要

• エントリーDOI: 10.2210/pdb5yqw/pdb
• 分子名称: Peptide ABC transporter, periplasmic peptide-binding protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE, ... (5 entities in total)
• 機能のキーワード: chitooligosaccharide-binding protein, vibrio harveyi, protein binding
• 由来する生物種: Vibrio harveyi (strain 1DA3)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61024.44

構造登録者

Suginta, W.,Sritho, N.,Ranok, A.,Kitaoku, Y.,Bulmer, D.M.,van den Berg, B.,Fukamizo, T. (登録日: 2017-11-08, 公開日: 2018-02-21, 最終更新日: 2024-11-20)

主引用文献

Suginta, W.,Sritho, N.,Ranok, A.,Bulmer, D.M.,Kitaoku, Y.,van den Berg, B.,Fukamizo, T.
Structure and function of a novel periplasmic chitooligosaccharide-binding protein from marineVibriobacteria.
J. Biol. Chem., 293:5150-5159, 2018

PubMed Abstract: Periplasmic solute-binding proteins in bacteria are involved in the active transport of nutrients into the cytoplasm. In marine bacteria of the genus , a chitooligosaccharide-binding protein (CBP) is thought to be the major solute-binding protein controlling the rate of chitin uptake in these bacteria. However, the molecular mechanism of the CBP involvement in chitin metabolism has not been elucidated. Here, we report the structure and function of a recombinant chitooligosaccharide-binding protein from , namely CBP, expressed in Isothermal titration calorimetry revealed that CBP strongly binds shorter chitooligosaccharides ((GlcNAc) , where = 2, 3, and 4) with affinities that are considerably greater than those for glycoside hydrolase family 18 and 19 chitinases but does not bind longer ones, including insoluble chitin polysaccharides. We also found that VhCBP comprises two domains with flexible linkers and that the domain-domain interface forms the sugar-binding cleft, which is not long extended but forms a small cavity. (GlcNAc) bound to this cavity, apparently triggering a closed conformation of CBP. Trp-363 and Trp-513, which stack against the two individual GlcNAc rings, likely make a major contribution to the high affinity of CBP for (GlcNAc) The strong chitobiose binding, followed by the conformational change of CBP, may facilitate its interaction with an active-transport system in the inner membrane of species.

PubMed: 29444825
DOI: 10.1074/jbc.RA117.001012

実験手法

X-RAY DIFFRACTION (1.36 Å)