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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DOI10.2210/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
Saleem-Batcha, R.,Keppler, M.,Kuge, M.,Andexer, J.N. (登録日: 2024-09-07, 公開日: 2025-07-16)
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: 39846220
DOI: 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)
構造検証レポート
Validation report summary of 9gp9
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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