5UB4

XAC2383 from Xanthomonas citri bound to phosphate

5UB4 の概要

• エントリーDOI: 10.2210/pdb5ub4/pdb
• 関連するPDBエントリー: 5UB3 5UB6 5UB7
• 分子名称: Phosphate-binding protein, CHLORIDE ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: periplasmic binding protein periplasmic sensor phosphate ion phosphonate-bd, metal binding protein
• 由来する生物種: Xanthomonas axonopodis pv. citri (strain 306)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62995.15

構造登録者

Teixeira, R.D.,Guzzo, C.R.,Farah, C.S. (登録日: 2016-12-20, 公開日: 2018-01-10, 最終更新日: 2024-03-06)

主引用文献

Teixeira, R.D.,Guzzo, C.R.,Arevalo, S.J.,Andrade, M.O.,Abrahao, J.,de Souza, R.F.,Farah, C.S.
A bipartite periplasmic receptor-diguanylate cyclase pair (XAC2383-XAC2382) in the bacteriumXanthomonas citri.
J. Biol. Chem., 293:10767-10781, 2018

PubMed Abstract: The second messenger cyclic diguanylate monophosphate (c-di-GMP) is a central regulator of bacterial lifestyle, controlling several behaviors, including the switch between sessile and motile states. The c-di-GMP levels are controlled by the interplay between diguanylate cyclases (DGCs) and phosphodiesterases, which synthesize and hydrolyze this second messenger, respectively. These enzymes often contain additional domains that regulate activity via binding of small molecules, covalent modification, or protein-protein interactions. A major challenge remains to understand how DGC activity is regulated by these additional domains or interaction partners in specific signaling pathways. Here, we identified a pair of co-transcribed genes ( and ) in the phytopathogenic, Gram-negative bacterium subsp. (Xac), whose mutations resulted in opposing motility phenotypes. We show that the periplasmic cache domain of XAC2382, a membrane-associated DGC, interacts with XAC2383, a periplasmic binding protein, and we provide evidence that this interaction regulates XAC2382 DGC activity. Moreover, we solved the crystal structure of XAC2383 with different ligands, indicating a preference for negatively charged phosphate-containing compounds. We propose that XAC2383 acts as a periplasmic sensor that, upon binding its ligand, inhibits the DGC activity of XAC2382. Of note, we also found that this previously uncharacterized signal transduction system is present in several other bacterial phyla, including Gram-positive bacteria. Phylogenetic analysis of homologs of the XAC2382-XAC2383 pair supports several independent origins that created new combinations of XAC2382 homologs with a conserved periplasmic cache domain with different cytoplasmic output module architectures.

PubMed: 29728456
DOI: 10.1074/jbc.RA118.003475

実験手法

X-RAY DIFFRACTION (2.09 Å)