1NDK
X-RAY STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE
1NDK の概要
| エントリーDOI | 10.2210/pdb1ndk/pdb |
| 分子名称 | NUCLEOSIDE DIPHOSPHATE KINASE (2 entities in total) |
| 機能のキーワード | transferase |
| 由来する生物種 | Dictyostelium discoideum |
| 細胞内の位置 | Cytoplasm: P22887 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 16781.33 |
| 構造登録者 | Janin, J.,Dumas, C.,Morera, S.,Lascu, I.,Veron, M. (登録日: 1993-07-15, 公開日: 1993-10-31, 最終更新日: 2024-02-14) |
| 主引用文献 | Dumas, C.,Lascu, I.,Morera, S.,Glaser, P.,Fourme, R.,Wallet, V.,Lacombe, M.L.,Veron, M.,Janin, J. X-ray structure of nucleoside diphosphate kinase. EMBO J., 11:3203-3208, 1992 Cited by PubMed Abstract: The X-ray structure of a point mutant of nucleoside diphosphate kinase (NDP kinase) from Dictyostelium discoideum has been determined to 2.2 A resolution. The enzyme is a hexamer made of identical subunits with a novel mononucleotide binding fold. Each subunit contains an alpha/beta domain with a four stranded, antiparallel beta-sheet. The topology is different from adenylate kinase, but identical to the allosteric domain of Escherichia coli ATCase regulatory subunits, which bind mononucleotides at an equivalent position. Dimer contacts between NDP kinase subunits within the hexamer are similar to those in ATCase. Trimer contacts involve a large loop of polypeptide chain that bears the site of the Pro----Ser substitution in Killer of prune (K-pn) mutants of the highly homologous Drosophila enzyme. Properties of Drosophila NDP kinase, the product of the awd developmental gene, and of the human enzyme, the product of the nm23 genes in tumorigenesis, are discussed in view of the three-dimensional structure and of possible interactions of NDP kinase with other nucleotide binding proteins. PubMed: 1324167主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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