4QS7
Arabidopsis Hexokinase 1 (AtHXK1) structure in glucose-bound form
4QS7 の概要
| エントリーDOI | 10.2210/pdb4qs7/pdb |
| 関連するPDBエントリー | 4QS8 4QS9 |
| 分子名称 | Hexokinase-1, beta-D-glucopyranose (3 entities in total) |
| 機能のキーワード | hexokinase, atp-dependent, sugar sensor, transferase |
| 由来する生物種 | Arabidopsis thaliana (mouse-ear cress, thale cress) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 51964.32 |
| 構造登録者 | |
| 主引用文献 | Feng, J.,Zhao, S.,Chen, X.,Wang, W.,Dong, W.,Chen, J.,Shen, J.-R.,Liu, L.,Kuang, T. Biochemical and structural study of Arabidopsis hexokinase 1 Acta Crystallogr.,Sect.D, 71:367-375, 2015 Cited by PubMed Abstract: Hexokinase 1 from Arabidopsis thaliana (AtHXK1) plays a dual role in glycolysis and sugar sensing for vital metabolic and physiological processes. The uncoupling of glucose signalling from glucose metabolism was demonstrated by the analysis of two mutants (AtHXK1(G104D) and AtHXK1(S177A)) that are catalytically inactive but still functional in signalling. In this study, substrate-binding experiments indicate that the two catalytically inactive mutants have a high affinity for glucose, and an ordered substrate-binding mechanism has been observed for wild-type AtHXK1. The structure of AtHXK1 was determined both in its inactive unliganded form and in its active glucose-bound form at resolutions of 1.8 and 2.0 Å, respectively. These structures reveal a domain rearrangement of AtHXK1 upon glucose binding. The 2.1 Å resolution structure of AtHXK1(S177A) in the glucose-bound form shows similar glucose-binding interactions as the wild type. A glucose-sensing network has been proposed based on these structures. Taken together, the results provide a structural explanation for the dual functions of AtHXK1. PubMed: 25664748DOI: 10.1107/S1399004714026091 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.001 Å) |
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