PDBsum entry 5yqw

Protein binding

PDB id: 5yqw

Contents

Protein chain

532 a.a.

Ligands

NAG-NAG

P4G ×2

Metals

_NI

Waters ×461

PDB id:

5yqw

Name:

Protein binding

Title:

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

Structure:

Peptide abc transporter, periplasmic peptide-binding protein. Chain: a. Synonym: chitooligosaccharide-binding protein. Engineered: yes

Source:

Vibrio harveyi (strain 1da3). Organism_taxid: 673519. Strain: 1da3. Gene: vme_26970. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.36Å R-factor: 0.197 R-free: 0.226

Authors:

W.Suginta,N.Sritho,A.Ranok,Y.Kitaoku,D.M.Bulmer,B.Van Den Berg, T.Fukamizo

Key ref:

W.Suginta et al. (2018). Structure and function of a novel periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria. J Biol Chem, 293, 5150-5159. PubMed id: 29444825

Date:

08-Nov-17 Release date: 21-Feb-18

Protein chain

D0XC84  (D0XC84_VIBH1) -

J Biol Chem 293:5150-5159 (2018)

PubMed id: 29444825

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

W.Suginta, N.Sritho, A.Ranok, D.M.Bulmer, Y.Kitaoku, B.van den Berg, T.Fukamizo.

ABSTRACT

Periplasmic solute-binding proteins in bacteria are involved in the active transport of nutrients into the cytoplasm. In marine bacteria of the genus Vibrio, 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 Vibrio harveyi, namely VhCBP, expressed in Escherichia coli Isothermal titration calorimetry revealed that VhCBP strongly binds shorter chitooligosaccharides ((GlcNAc)