4AQK
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase in complex with ADP and IP6
4AQK の概要
| エントリーDOI | 10.2210/pdb4aqk/pdb |
| 関連するPDBエントリー | 2XAL 2XAM 2XAN 2XAO 2XAR |
| 分子名称 | INOSITOL-PENTAKISPHOSPHATE 2-KINASE, INOSITOL HEXAKISPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| 機能のキーワード | transferase, inositide kinase, phytic acid, inositide signalling, insp5 2-k |
| 由来する生物種 | ARABIDOPSIS THALIANA (THALE CRESS) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 52498.16 |
| 構造登録者 | I Banos-Sanz, J.,Sanz-Aparicio, J.,Gonzalez, B. (登録日: 2012-04-18, 公開日: 2012-05-02, 最終更新日: 2023-12-20) |
| 主引用文献 | Banos-Sanz, J.I.,Sanz-Aparicio, J.,Brearley, C.A.,Gonzalez, B. Expression, Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of the Apo Form of Insp5 2-K from Arabidopsis Thaliana. Acta Crystallogr.,Sect.F, 68:701-, 2012 Cited by PubMed Abstract: Inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IP(5) 2-K) is a key enzyme that catalyzes the synthesis of phytic acid (IP(6)) from inositol 1,3,4,5,6-pentakisphosphate (IP(5)) and ATP. The first structure of IP(5) 2-K, that from Arabidopsis thaliana, has been solved previously; it only crystallized in the presence of inositol, either the substrate IP(5) or the product IP(6), and failed to crystallize in its free state (without inositol). Based on structural analysis, a point mutation of IP(5) 2-K (W129A) has been produced in order to overcome this limitation and obtain information about protein conformational changes upon substrate binding. Here, the production and crystallization of W129A IP(5) 2-K in its free state and with bound nucleotide is described. These crystals differed from the native crystals and belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 66.00, b = 68.23, c = 105.80 Å and a = 63.06, b = 71.80, c = 100.23 Å, respectively. The crystals diffracted to resolutions of 2.22 Å (apo) and 2.05 Å (nucleotide bound) using synchrotron radiation and contained one molecule per asymmetric unit. The structures have been determined using the molecular-replacement method and refinement is being undertaken. PubMed: 22684075DOI: 10.1107/S1744309112017307 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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