6i7w

Structure of the periplasmic binding protein (PBP) AccA in complex with 2-glucose-2-O-lactic acid phosphate (G2LP) from Agrobacterium fabrum C58

spinqualitylabelsall models 6i7w, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i7w is a 1 chain structure with sequence from Agrobacterium fabrum str. C58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: H6Q, H6Z, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q52012_AGRFC Publication Abstract from PubMed The first non-natural derivative of the rare d-glucose-2-phosphate (G2P), namely glucose-2-(O-lactic acid phosphate) (G2LP), has been synthesized. When used as sole carbon source, G2LP enables bacterial growth of the plant pathogenic strain Agrobacterium fabrum C58 (formerly referred to as Agrobacterium tumefaciens). X-ray crystallography and affinity measurements investigations reveal that G2LP binds the periplasmic binding protein (PBP) AccA similarly to the natural compounds and with the same affinity. Moreover, enzymatic assays show that it is able to serve as substrate of the phosphodiesterase AccF. The properties found for G2LP demonstrate that the very unusual glucose-2-phosphoryl residue, present in G2LP, can be used as structural feature for designing non-natural systems fully compatible with the Acc cascade of A. fabrum. Synthesis of a non-natural glucose-2-phosphate ester able to dupe the acc system of Agrobacterium fabrum.,Li SZ, Vigouroux A, Ahmar M, El Sahili A, Soulere L, Sago L, Cornu D, Morera S, Queneau Y Org Biomol Chem. 2019 Jan 31;17(5):1090-1096. doi: 10.1039/c8ob03086c. PMID:30632589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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