1HW6
CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE
1HW6 の概要
エントリーDOI | 10.2210/pdb1hw6/pdb |
関連するPDBエントリー | 1A80 |
分子名称 | 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total) |
機能のキーワード | aldo-keto reductase, tim barrel, oxidoreductase |
由来する生物種 | Corynebacterium sp. |
細胞内の位置 | Cytoplasm: P06632 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 30271.18 |
構造登録者 | |
主引用文献 | Sanli, G.,Blaber, M. Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor. J.Mol.Biol., 309:1209-1218, 2001 Cited by PubMed Abstract: A 1.9 A resolution X-ray structure of the apo-form of Corynebacterium 2,5-diketo-d-gluconic acid reductase A (2,5-DKGR A), a member of the aldo-keto reductase superfamily, has been determined by molecular replacement using the NADPH-bound form of the same enzyme as the search model. 2,5-DKGR A catalyzes the NADPH-dependent stereo-specific reduction of 2,5-diketo-d-gluconate (2,5-DKG) to 2-keto-l-gulonate, a precursor in the industrial production of vitamin C. An atomic-resolution structure for the apo-form of the enzyme, in conjunction with our previously reported high-resolution X-ray structure for the holo-enzyme and holo/substrate model, allows a comparative analysis of structural changes that accompany cofactor binding. The results show that regions of the active site undergo coordinated conformational changes of up to 8 A. These conformational changes result in the organization and structural rearrangement of residues associated with substrate binding and catalysis. Thus, NADPH functions not only to provide a hydride ion for catalytic reduction, but is also a critical structural component for formation of a catalytically competent form of DKGR A. PubMed: 11399090DOI: 10.1006/jmbi.2001.4739 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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