6HLZ

Structure in C2 form of the PBP AgtB from A.tumefacien R10 in complex with agropinic acid

6HLZ の概要

• エントリーDOI: 10.2210/pdb6hlz/pdb
• 分子名称: Agropine permease, 1,2-ETHANEDIOL, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE, ... (7 entities in total)
• 機能のキーワード: periplasmic binding protein, abc transporter, transport protein
• 由来する生物種: Agrobacterium tumefaciens LBA4213 (Ach5)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80532.55

構造登録者

Morera, S.,Marty, L.,Vigouroux, A. (登録日: 2018-09-11, 公開日: 2018-12-26, 最終更新日: 2024-01-24)

主引用文献

Marty, L.,Vigouroux, A.,Aumont-Nicaise, M.,Pelissier, F.,Meyer, T.,Lavire, C.,Dessaux, Y.,Morera, S.
Structural basis for two efficient modes of agropinic acid opine import into the bacterial pathogenAgrobacterium tumefaciens.
Biochem. J., 476:165-178, 2019

PubMed Abstract: pathogens genetically modify their host plants to drive the synthesis of opines in plant tumors. The mannityl-opine family encompasses mannopine, mannopinic acid, agropine and agropinic acid. These opines serve as nutrients and are imported into bacteria via periplasmic-binding proteins (PBPs) in association with ABC transporters. Structural and affinity data on agropine and agropinic acid opines bound to PBPs are currently lacking. Here, we investigated the molecular basis of AgtB and AgaA, proposed as the specific PBP for agropine and agropinic acid import, respectively. Using genetic approaches and affinity measurements, we identified AgtB and its transporter as responsible for agropine uptake in agropine-assimilating agrobacteria. Nonetheless, we showed that AgtB binds agropinic acid with a higher affinity than agropine, and we structurally characterized the agropinic acid-binding mode through three crystal structures at 1.4, 1.74 and 1.9 Å resolution. In the crystallization time course, obtaining a crystal structure of AgtB with agropine was unsuccessful due to the spontaneous lactamization of agropine into agropinic acid. AgaA binds agropinic acid only with a similar affinity in nanomolar range as AgtB. The structure of AgaA bound to agropinic acid at 1.65 Å resolution defines a different agropinic acid-binding signature. Our work highlights the structural and functional characteristics of two efficient agropinic acid assimilation pathways, of which one is also involved in agropine assimilation.

PubMed: 30552142
DOI: 10.1042/BCJ20180861

実験手法

X-RAY DIFFRACTION (1.89 Å)