7O4X
Crystal structure of the PII-like protein PotN from Lentilactobacillus hilgardii
Summary for 7O4X
Entry DOI | 10.2210/pdb7o4x/pdb |
Descriptor | Nitrogen regulatory protein P-II, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | signaling protein |
Biological source | Lactobacillus brevis subsp. gravesensis ATCC 27305 |
Total number of polymer chains | 1 |
Total formula weight | 14187.10 |
Authors | Heim, C.,Hartmann, M.D. (deposition date: 2021-04-07, release date: 2022-04-20, Last modification date: 2024-01-31) |
Primary citation | 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 Cited by 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: 35285159DOI: 10.1111/febs.16431 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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