8CHC

PBP AccA from A. vitis S4 in complex with Agrocinopine D-like

Summary for 8CHC

• Entry DOI: 10.2210/pdb8chc/pdb
• Descriptor: Agrocinopine utilization periplasmic binding protein AccA, Agrocinopine D-like (C2-C2 linked; with two alpha-D-glucopyranoses) (3 entities in total)
• Functional Keywords: periplasmic binding protein, solute binding protein, transport protein
• Biological source: Allorhizobium ampelinum S4
• Total number of polymer chains: 1
• Total formula weight: 57074.71

Authors

Morera, S.,Vigouroux, A.,Deicsics, G. (deposition date: 2023-02-07, release date: 2024-01-24, Last modification date: 2024-02-07)

Primary citation

Morera, S.,Vigouroux, A.,Aumont-Nicaise, M.,Ahmar, M.,Meyer, T.,El Sahili, A.,Deicsics, G.,Gonzalez-Mula, A.,Li, S.,Dore, J.,Sirigu, S.,Legrand, P.,Penot, C.,Andre, F.,Faure, D.,Soulere, L.,Queneau, Y.,Vial, L.
A highly conserved ligand-binding site for AccA transporters of antibiotic and quorum-sensing regulator in Agrobacterium leads to a different specificity.
Biochem.J., 481:93-117, 2024

PubMed Abstract: Plants genetically modified by the pathogenic Agrobacterium strain C58 synthesize agrocinopines A and B, whereas those modified by the pathogenic strain Bo542 produce agrocinopines C and D. The four agrocinopines (A, B, C and D) serve as nutrients by agrobacteria and signaling molecule for the dissemination of virulence genes. They share the uncommon pyranose-2-phosphate motif, represented by the l-arabinopyranose moiety in agrocinopines A/B and the d-glucopyranose moiety in agrocinopines C/D, also found in the antibiotic agrocin 84. They are imported into agrobacterial cytoplasm via the Acc transport system, including the solute-binding protein AccA coupled to an ABC transporter. We have previously shown that unexpectedly, AccA from strain C58 (AccAC58) recognizes the pyranose-2-phosphate motif present in all four agrocinopines and agrocin 84, meaning that strain C58 is able to import agrocinopines C/D, originating from the competitor strain Bo542. Here, using agrocinopine derivatives and combining crystallography, affinity and stability measurements, modeling, molecular dynamics, in vitro and vivo assays, we show that AccABo542 and AccAC58 behave differently despite 75% sequence identity and a nearly identical ligand binding site. Indeed, strain Bo542 imports only compounds containing the d-glucopyranose-2-phosphate moiety, and with a lower affinity compared with strain C58. This difference in import efficiency makes C58 more competitive than Bo542 in culture media. We can now explain why Agrobacterium/Allorhizobium vitis strain S4 is insensitive to agrocin 84, although its genome contains a conserved Acc transport system. Overall, our work highlights AccA proteins as a case study, for which stability and dynamics drive specificity.

PubMed: 38058289
DOI: 10.1042/BCJ20230273

Experimental method

X-RAY DIFFRACTION (1.679 Å)