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7O4X

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

Summary for 7O4X
Entry DOI10.2210/pdb7o4x/pdb
DescriptorNitrogen regulatory protein P-II, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordssignaling protein
Biological sourceLactobacillus brevis subsp. gravesensis ATCC 27305
Total number of polymer chains1
Total formula weight14187.10
Authors
Heim, C.,Hartmann, M.D. (deposition date: 2021-04-07, release date: 2022-04-20, Last modification date: 2024-01-31)
Primary citationIskhakova, 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: 35285159
DOI: 10.1111/febs.16431
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

227344

数据于2024-11-13公开中

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