Periplasmic solute-binding proteins: Structure classification and chitooligosaccharide recognition
| Autor: | Wipa Suginta, Tamo Fukamizo, Yoshihito Kitaoku |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Oligosaccharides
Chitin 02 engineering and technology Plasma protein binding Biochemistry 03 medical and health sciences Marine bacteriophage Bacterial Proteins Structural Biology Inner membrane Thermotoga maritima Amino Acid Sequence Molecular Biology Peptide sequence Vibrio 030304 developmental biology Chitosan 0303 health sciences biology Chemistry General Medicine Periplasmic space 021001 nanoscience & nanotechnology biology.organism_classification Periplasmic Binding Proteins 0210 nano-technology Bacterial outer membrane Protein Binding |
| Zdroj: | International Journal of Biological Macromolecules. 128:985-993 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2019.02.064 |
| Popis: | 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, I V. 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect