Periplasmic solute-binding proteins: Structure classification and chitooligosaccharide recognition

Tamo Fukamizo, Yoshihito Kitaoku, Wipa Suginta

Research output: Contribution to journalReview articlepeer-review

20 Citations (Scopus)


Periplasmic solute-binding proteins (SBPs) serve as molecular shuttles that assist the transport of small solutes from the outer membrane to the inner membrane of all Gram-negative bacteria. Based on the available crystal structures, SBPs are classified into seven clusters, A-G, and are further divided into subclusters, IV. This minireview is focused on the classification, structure and substrate specificity of a distinct class of SBPs specific for chitooligosaccharides (CBPs). To date, only two structures of CBP homologues, VhCBP and VcCBP, have been reported in the marine Vibrio species, with exposition of their limited function. The Vibrio CBPs are structurally classified as cluster C/subcluster IV SBPs that exclusively recognize β-1,4- or β-1,3-linked linear oligosaccharides. The overall structural feature of the Vibrios CBPs is most similar to the cellobiose-binding orthologue from the hyperthermophilic bacterium Thermotoga maritima. This similarity provides an opportunity to engineer the substrate specificity of the proteins and to control the uptake of chitinous and cellulosic nutrients in marine bacteria.

Original languageEnglish
Pages (from-to)985-993
Number of pages9
JournalInternational Journal of Biological Macromolecules
Publication statusPublished - May 1 2019
Externally publishedYes


  • Amino Acid Sequence
  • Bacterial Proteins/chemistry
  • Chitin/analogs & derivatives
  • Periplasmic Binding Proteins/chemistry
  • Protein Binding
  • Thermotoga maritima
  • Vibrio


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