Structure of a Polyisoprenoid Binding Domain from Saccharophagus Degradans Implicated in Plant Cell Wall Breakdown
Vincent, F., Dalmolin, D., Weiner, R.M., Bourne, Y., Henrissat, B.(2010) FEBS Lett 584: 1577
- PubMed: 20227408 
- DOI: https://doi.org/10.1016/j.febslet.2010.03.015
- Primary Citation of Related Structures:  
2X32, 2X34 - PubMed Abstract: 
Saccharophagus degradans belongs to a recently discovered group of marine bacteria equipped with an arsenal of sugar cleaving enzymes coupled to carbohydrate-binding domains to degrade various insoluble complex polysaccharides. The modular Sde-1182 protein consists of a family 2 carbohydrate binding module linked to a X158 domain of unknown function. The 1.9 A and 1.55 A resolution crystal structures of the isolated X158 domain bound to the two related polyisoprenoid molecules, ubiquinone and octaprenyl pyrophosphate, unveil a beta-barrel architecture reminiscent of the YceI-like superfamily that resembles the architecture of the lipocalin fold. This unprecedented association coupling oxidoreduction and carbohydrate recognition events may have implications for effective nutrient uptake in the marine environment.
- Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS and Aix-Marseille Universities, Marseille, France. florence.vincent@afmb.univ-mrs.fr
Organizational Affiliation: