A structural model for (GlcNAc)₂ translocation via a periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria.

ABSTRACT: VhCBP is a periplasmic chitooligosaccharide-binding protein mainly responsible for translocation of the chitooligosaccharide (GlcNAc)₂ across the double membranes of marine bacteria. However, structural and thermodynamic understanding of the sugar-binding/-release processes of VhCBP is relatively less. VhCBP displayed the greatest affinity toward (GlcNAc)₂, with lower affinity for longer-chain chitooligosaccharides [(GlcNAc)_3-4]. (GlcNAc)₄ partially occupied the closed sugar-binding groove, with two reducing-end GlcNAc units extending beyond the sugar-binding groove and barely characterized by weak electron density. Mutation of three conserved residues (Trp³⁶³, Asp³⁶⁵, and Trp⁵¹³) to Ala resulted in drastic decrea

SUBMITTER: Kitaoku Y 

PROVIDER: S-EPMC8449061 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature