2X32

Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown

Summary for 2X32

• Entry DOI: 10.2210/pdb2x32/pdb
• Related: 2X34
• Descriptor: CELLULOSE-BINDING PROTEIN, (2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-OCTAMETHYLDOTRIACONTA-2,6,10,14,18,22,26,30-OCTAENYL TRIHYDROGEN DIPHOSPHATE, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: carbohydrate-binding protein, oxidoreduction, marine bacteria, polyisoprenoid transport
• Biological source: SACCHAROPHAGUS DEGRADANS
• Total number of polymer chains: 2
• Total formula weight: 40306.72

Authors

Vincent, F.,Dal Molin, D.,Weiner, R.M.,Bourne, Y.,Henrissat, B. (deposition date: 2010-01-19, release date: 2010-03-23, Last modification date: 2023-12-20)

Primary citation

Vincent, F.,Dalmolin, D.,Weiner, R.M.,Bourne, Y.,Henrissat, B.
Structure of a Polyisoprenoid Binding Domain from Saccharophagus Degradans Implicated in Plant Cell Wall Breakdown
FEBS Lett., 584:1577-, 2010

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.

PubMed: 20227408
DOI: 10.1016/J.FEBSLET.2010.03.015

Experimental method

X-RAY DIFFRACTION (1.55 Å)