9egi

Crystal Structure of EgtUC binding domain mutant T274G bound to L-Ergothioneine from S. pneumoniae

spinqualitylabelsall models 9egi, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9egi is a 2 chain structure with sequence from Streptococcus pneumoniae D39. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: LW8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EGTUB_STRP2 Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant (PubMed:36481738). Responsible for the translocation of the substrate across the membrane (PubMed:36481738). Also contains a C-terminal periplasmic solute-binding domain (SBD) which binds to EGT with sub-micromolar affinity (PubMed:36481738). Binds L-hercynine about 10,000-fold less tightly than EGT (PubMed:36481738). Cannot bind the structurally similar compounds L-histidine, proline-betaine, choline, ectoine, carnitine or dimethylpropiothetin (PubMed:36481738).

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