6h7d

Crystal Structure of A. thaliana Sugar Transport Protein 10 in complex with glucose in the outward occluded state

spinqualitylabelsall models 6h7d, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h7d is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, OLC, P33, PO4 Gene: STP10, At3g19940, MPN9.19 (ARATH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [STP10_ARATH] Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Publication Abstract from PubMed 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 A 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. Crystal structure of the plant symporter STP10 illuminates sugar uptake mechanism in monosaccharide transporter superfamily.,Paulsen PA, Custodio TF, Pedersen BP Nat Commun. 2019 Jan 24;10(1):407. doi: 10.1038/s41467-018-08176-9. PMID:30679446 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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