7O4X

Crystal structure of the PII-like protein PotN from Lentilactobacillus hilgardii

7O4X の概要

• エントリーDOI: 10.2210/pdb7o4x/pdb
• 分子名称: Nitrogen regulatory protein P-II, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: signaling protein
• 由来する生物種: Lactobacillus brevis subsp. gravesensis ATCC 27305
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14187.10

構造登録者

Heim, C.,Hartmann, M.D. (登録日: 2021-04-07, 公開日: 2022-04-20, 最終更新日: 2024-01-31)

主引用文献

Iskhakova, Z.I.,Zhuravleva, D.E.,Heim, C.,Hartmann, M.D.,Laykov, A.V.,Forchhammer, K.,Kayumov, A.R.
PotN represents a novel energy-state sensing PII subfamily, occurring in firmicutes.
Febs J., 289:5305-5321, 2022

PubMed Abstract: PII proteins are signal processor proteins that regulate the cellular metabolism of Bacteria, Archea and plant chloroplasts typically in response to the cellular nitrogen status. Here, we report the first biochemical characterization of a novel PII-like protein PotN from Lentilactobacillus hilgardii. PotN is encoded in an operon together with the potABCD genes, encoding the ABC transporter for spermidine/putrescine. Like canonical PII proteins, the native PotN has a trimeric structure and competitively binds ATP and ADP, but it does not bind 2-oxoglutarate. Immunoprecipitation and pull-down experiments revealed that PotN is associated in vivo with the transcriptional regulator GlnR and the beta-subunit of pyruvate/2-oxoglutarate/acetoin dehydrogenase AcoB. Moreover, in vitro assays revealed that the ATPase domain of PotA also is able to interact with PotN. Interaction analyses demonstrated that PotN preferentially associates with PotA in the ADP state, whereas it binds to GlnR at elevated ATP levels. This suggests that PotN regulates the transport of polyamines and GlnR-dependent gene expression in response to the energy availability for the cell.

PubMed: 35285159
DOI: 10.1111/febs.16431

実験手法

X-RAY DIFFRACTION (1.65 Å)