6H7D
Crystal Structure of A. thaliana Sugar Transport Protein 10 in complex with glucose in the outward occluded state
Summary for 6H7D
| Entry DOI | 10.2210/pdb6h7d/pdb |
| Descriptor | Sugar transport protein 10, beta-D-glucopyranose, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, ... (6 entities in total) |
| Functional Keywords | membrane protein, alpha-helical protein, sugar transport, protoin/sugar symporter, major facilitator |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 59320.85 |
| Authors | Pedersen, B.P.,Paulsen, P.A.,Custodio, T.F. (deposition date: 2018-07-31, release date: 2019-02-06, Last modification date: 2024-10-09) |
| Primary citation | Paulsen, P.A.,Custodio, T.F.,Pedersen, B.P. Crystal structure of the plant symporter STP10 illuminates sugar uptake mechanism in monosaccharide transporter superfamily. Nat Commun, 10:407-407, 2019 Cited by PubMed Abstract: Plants are dependent on controlled sugar uptake for correct organ development and sugar storage, and apoplastic sugar depletion is a defense strategy against microbial infections like rust and mildew. Uptake of glucose and other monosaccharides is mediated by Sugar Transport Proteins, proton-coupled symporters from the Monosaccharide Transporter (MST) superfamily. We present the 2.4 Å structure of Arabidopsis thaliana high affinity sugar transport protein, STP10, with glucose bound. The structure explains high affinity sugar recognition and suggests a proton donor/acceptor pair that links sugar transport to proton translocation. It contains a Lid domain, conserved in all STPs, that locks the mobile transmembrane domains through a disulfide bridge, and creates a protected environment which allows efficient coupling of the proton gradient to drive sugar uptake. The STP10 structure illuminates fundamental principles of sugar transport in the MST superfamily with implications for both plant antimicrobial defense, organ development and sugar storage. PubMed: 30679446DOI: 10.1038/s41467-018-08176-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
