9GP9
Crystal Structure of Polyphosphate kinase 2-II (PPK2-II) from Lysinibacillus fusiformis bound to ADP (form I)
9GP9 の概要
| エントリーDOI | 10.2210/pdb9gp9/pdb |
| 関連するPDBエントリー | 9GIA 9GOR 9GP6 |
| 分子名称 | Polyphosphate kinase, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION, ... (4 entities in total) |
| 機能のキーワード | polyphosphate kinase 2 (ppk2); phosphotransferase; enzyme structure; kinase; polyphosphate., transferase |
| 由来する生物種 | Lysinibacillus fusiformis |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 69534.09 |
| 構造登録者 | |
| 主引用文献 | Kuge, M.,Keppler, M.,Friedrich, F.,Saleem-Batcha, R.,Winter, J.,Prucker, I.,Germer, P.,Gerhardt, S.,Einsle, O.,Jung, M.,Jessen, H.J.,Andexer, J.N. Structural Insights into Broad-Range Polyphosphate Kinase 2-II Enzymes Applicable for Pyrimidine Nucleoside Diphosphate Synthesis. Chembiochem, 26:e202400970-e202400970, 2025 Cited by PubMed Abstract: Polyphosphate kinases (PPK) play crucial roles in various biological processes, including energy storage and stress responses, through their interaction with inorganic polyphosphate (polyP) and the intracellular nucleotide pool. Members of the PPK family 2 (PPK2s) catalyse polyP-consuming phosphorylation of nucleotides. In this study, we characterised two PPK2 enzymes from Bacillus cereus (BcPPK2) and Lysinibacillus fusiformis (LfPPK2) to investigate their substrate specificity and potential for selective nucleotide synthesis. Both enzymes exhibited a broad substrate scope, selectively converting over 85 % of pyrimidine nucleoside monophosphates (NMPs) to nucleoside diphosphates (NDPs), while nucleoside triphosphate (NTP) formation was observed only with purine NMPs. Preparative enzymatic synthesis of cytidine diphosphate (CDP) was applied to achieve an yield of 49 %. Finally, structural analysis of five crystal structures of BcPPK2 and LfPPK2 provided insights into their active sites and substrate interactions. This study highlights PPK2-II enzymes as promising biocatalysts for the efficient and selective synthesis of pyrimidine NDPs. PubMed: 39846220DOI: 10.1002/cbic.202400970 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.88 Å) |
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