9fw6

A ternary complex of plant adenosine kinase 1 from moss Physcomitrella patens (PpADK1) with adenosine and ADP

spinqualitylabelsall models 9fw6, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9fw6 is a 2 chain structure with sequence from Physcomitrium patens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.73Å Ligands: ADN, ADP, EDO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ADK_PHYPA ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Can also act on the cytokinin isopentenyladenosine to produce isopentenyladenosine monophosphate. Publication Abstract from PubMed Adenosine undergoes ATP-dependent phosphorylation catalyzed by adenosine kinase (ADK). In plants, ADK also phosphorylates cytokinin ribosides, transport forms of the hormone. Here, we investigated the substrate preferences, oligomeric states and structures of ADKs from moss (Physcomitrella patens) and maize (Zea mays) alongside metabolomic and phenotypic analyses. We showed that dexamethasone-inducible ZmADK overexpressor lines in Arabidopsis can benefit from a higher number of lateral roots and larger root areas under nitrogen starvation. We discovered that maize and moss enzymes can form dimers upon increasing protein concentration, setting them apart from the monomeric human and protozoal ADKs. Structural and kinetic analyses revealed a catalytically inactive unique dimer. Within the dimer, both active sites are mutually blocked. The activity of moss ADKs, exhibiting a higher propensity to dimerize, was tenfold lower compared to maize ADKs. Two monomeric structures in a ternary complex highlight the characteristic transition from an open to a closed state upon substrate binding. This suggests that the oligomeric state switch can modulate the activity of moss ADKs and likely other plant ADKs. Moreover, dimer association represents a novel negative feedback mechanism, helping to maintain steady levels of adenosine and AMP. A monomer-dimer switch modulates the activity of plant adenosine kinase.,Kopecny DJ, Vigouroux A, Belicek J, Kopecna M, Koncitikova R, Friedecka J, Mik V, Supikova K, Humplik JF, Le Berre M, Plancqueel S, Strnad M, von Schwartzenberg K, Novak O, Morera S, Kopecny D J Exp Bot. 2025 Mar 10:eraf094. doi: 10.1093/jxb/eraf094. PMID:40063605 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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