7S6G

Crystal structure of PhnD from Synechococcus MITS9220 in complex with phosphate

7S6G の概要

• エントリーDOI: 10.2210/pdb7s6g/pdb
• 分子名称: Phosphonate ABC type transporter/ substrate binding component, CHLORIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: substrate-binding protein, marine cyanobacteria, phosphate-binding protein, transport protein
• 由来する生物種: Synechococcus sp. MIT S9220
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30788.97

構造登録者

Shah, B.S.,Mikolajek, H.,Orr, C.M.,Mykhaylyk, V.,Owens, R.J.,Paulsen, I.T. (登録日: 2021-09-14, 公開日: 2021-10-27, 最終更新日: 2024-05-22)

主引用文献

Shah, B.S.,Ford, B.A.,Varkey, D.,Mikolajek, H.,Orr, C.,Mykhaylyk, V.,Owens, R.J.,Paulsen, I.T.
Marine picocyanobacterial PhnD1 shows specificity for various phosphorus sources but likely represents a constitutive inorganic phosphate transporter.
Isme J, 17:1040-1051, 2023

PubMed Abstract: Despite being fundamental to multiple biological processes, phosphorus (P) availability in marine environments is often growth-limiting, with generally low surface concentrations. Picocyanobacteria strains encode a putative ABC-type phosphite/phosphate/phosphonate transporter, phnDCE, thought to provide access to an alternative phosphorus pool. This, however, is paradoxical given most picocyanobacterial strains lack known phosphite degradation or carbon-phosphate lyase pathway to utilise alternate phosphorus pools. To understand the function of the PhnDCE transport system and its ecological consequences, we characterised the PhnD1 binding proteins from four distinct marine Synechococcus isolates (CC9311, CC9605, MITS9220, and WH8102). We show the Synechococcus PhnD1 proteins selectively bind phosphorus compounds with a stronger affinity for phosphite than for phosphate or methyl phosphonate. However, based on our comprehensive ligand screening and growth experiments showing Synechococcus strains WH8102 and MITS9220 cannot utilise phosphite or methylphosphonate as a sole phosphorus source, we hypothesise that the picocyanobacterial PhnDCE transporter is a constitutively expressed, medium-affinity phosphate transporter, and the measured affinity of PhnD1 to phosphite or methyl phosphonate is fortuitous. Our MITS9220_PhnD1 structure explains the comparatively lower affinity of picocyanobacterial PhnD1 for phosphate, resulting from a more limited H-bond network. We propose two possible physiological roles for PhnD1. First, it could function in phospholipid recycling, working together with the predicted phospholipase, TesA, and alkaline phosphatase. Second, by having multiple transporters for P (PhnDCE and Pst), picocyanobacteria could balance the need for rapid transport during transient episodes of higher P availability in the environment, with the need for efficient P utilisation in typical phosphate-deplete conditions.

PubMed: 37087502
DOI: 10.1038/s41396-023-01417-w

実験手法

X-RAY DIFFRACTION (2.02 Å)