8C6W

PBP AccA from A. tumefaciens Bo542 in apoform 1

8C6W の概要

• エントリーDOI: 10.2210/pdb8c6w/pdb
• 関連するPDBエントリー: 8C6R 8C6U
• 分子名称: Agrocinopine utilization periplasmic binding protein AccA (2 entities in total)
• 機能のキーワード: periplasmic binding protein, solute binding protein, transport protein
• 由来する生物種: Agrobacterium tumefaciens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112587.50

構造登録者

Morera, S.,Vigouroux, A.,Legrand, P. (登録日: 2023-01-12, 公開日: 2024-01-24, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)