6I7W

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

Summary for 6I7W

• Entry DOI: 10.2210/pdb6i7w/pdb
• Related: 4RA1
• Descriptor: ABC transporter, substrate binding protein (Agrocinopines A and B), 2-O-[(R)-{[(2S)-1,1-dihydroxypropan-2-yl]oxy}(hydroxy)phosphoryl]-beta-D-glucopyranose, 2-O-[(R)-{[(2S)-1,1-dihydroxypropan-2-yl]oxy}(hydroxy)phosphoryl]-alpha-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: transport protein
• Biological source: Agrobacterium fabrum str. C58
• Total number of polymer chains: 1
• Total formula weight: 57869.52

Authors

Morera, S.,Vigouroux, A.,El Sahili, A. (deposition date: 2018-11-19, release date: 2019-01-23, Last modification date: 2024-01-24)

Primary citation

Li, S.Z.,Vigouroux, A.,Ahmar, M.,El Sahili, A.,Soulere, L.,Sago, L.,Cornu, D.,Morera, S.,Queneau, Y.
Synthesis of a non-natural glucose-2-phosphate ester able to dupe the acc system of Agrobacterium fabrum.
Org. Biomol. Chem., 17:1090-1096, 2019

PubMed Abstract: 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.

PubMed: 30632589
DOI: 10.1039/c8ob03086c

Experimental method

X-RAY DIFFRACTION (1.8 Å)