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1W7W

Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase: identification of residues involved in serine phosphorylation and oligomerization.

1W7W の概要
エントリーDOI10.2210/pdb1w7w/pdb
分子名称NUCLEOSIDE DIPHOSPHATE KINASE (2 entities in total)
機能のキーワードmitochondrial nucleoside diphosphate kinase, ndpk3, pisum sativum, transferase, kinase
由来する生物種PISUM SATIVUM (PEA)
タンパク質・核酸の鎖数6
化学式量合計124334.42
構造登録者
Johansson, M.,MacKenzie-Hose, A.,Andersson, I.,Knorpp, C. (登録日: 2004-09-13, 公開日: 2004-10-22, 最終更新日: 2023-12-13)
主引用文献Johansson, M.,Mackenzie-Hose, A.,Andersson, I.,Knorpp, C.
Structure and Mutational Analysis of a Plant Mitochondrial Nucleoside Diphosphate Kinase: Identification of Residues Involved in Serine Phosphorylation and Oligomerisation
Plant Physiol., 136:3034-, 2004
Cited by
PubMed Abstract: We report the first crystal structure of a plant (Pisum sativum L. cv Oregon sugarpod) mitochondrial nucleoside diphosphate kinase. Similar to other eukaryotic nucleoside diphosphate kinases, the plant enzyme is a hexamer; the six monomers in the asymmetric unit are arranged as trimers of dimers. Different functions of the kinase have been correlated with the oligomeric structure and the phosphorylation of Ser residues. We show that the occurrence of Ser autophosphorylation depends on enzymatic activity. The mutation of the strictly conserved Ser-119 to Ala reduced the Ser phosphorylation to about one-half of that observed in wild type with only a modest change of enzyme activity. We also show that mutating another strictly conserved Ser, Ser-69, to Ala reduces the enzyme activity to 6% and 14% of wild-type using dCDP and dTDP as acceptors, respectively. Changes in the oligomerization pattern of the S69A mutant were observed by cross-linking experiments. A reduction in trimer formation and a change in the dimer interaction could be detected with a concomitant increase of tetramers. We conclude that the S69 mutant is involved in the stabilization of the oligomeric state of this plant nucleoside diphosphate kinase.
PubMed: 15466238
DOI: 10.1104/PP.104.044040
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 1w7w
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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