8BFY

ABC transporter binding protein CebE from Streptomyces scabiei in complex with cellotriose

Summary for 8BFY

• Entry DOI: 10.2210/pdb8bfy/pdb
• Related PRD ID: PRD_900021
• Descriptor: Putative secreted cellobiose-binding (Transport system associated), beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total)
• Functional Keywords: abc transporter, maltose binding protein, carbohydrate
• Biological source: Streptomyces scabiei
• Total number of polymer chains: 1
• Total formula weight: 46449.52

Authors

Rigali, S.,Jourdan, S.,Kerff, F. (deposition date: 2022-10-27, release date: 2023-02-01, Last modification date: 2024-11-13)

Primary citation

Kerff, F.,Jourdan, S.,Francis, I.M.,Deflandre, B.,Ribeiro Monteiro, S.,Stulanovic, N.,Loria, R.,Rigali, S.
Common scab disease: structural basis of elicitor recognition in pathogenic Streptomyces species.
Microbiol Spectr, 11:e0197523-e0197523, 2023

PubMed Abstract: Common scab is a disease caused by a few species that affects important root and tuber crops including potato, beet, radish, and parsnip, resulting in major economic losses worldwide. In this work, we unveiled the molecular basis of host recognition by these pathogens by solving the structure of the sugar-binding protein CebE of in complex with cellotriose, the main elicitor of the pathogenic lifestyle of these bacteria. We further revealed that the signaling pathway from CebE-mediated transport of cellotriose is conserved in all pathogenic species except which causes soft rot disease in sweet potatoes. Our work also provides the structural basis of the uptake of cellobiose and cellotriose in saprophytic species, the first step activating the expression of the enzymatic system degrading the most abundant polysaccharide on earth, cellulose.

PubMed: 37791952
DOI: 10.1128/spectrum.01975-23

Experimental method

X-RAY DIFFRACTION (1.55 Å)