2YQC
Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the apo-like form
2YQC の概要
| エントリーDOI | 10.2210/pdb2yqc/pdb |
| 関連するPDBエントリー | 2YQH 2YQJ 2YQS |
| 分子名称 | UDP-N-acetylglucosamine pyrophosphorylase, MAGNESIUM ION, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | pyrophosphorylase, n-acetylglucosamine, uridine-diphospho-n-acetylglucosamine, n-acetylglucosamine-1-phosphate, candida albicans, transferase |
| 由来する生物種 | Candida albicans |
| 細胞内の位置 | Cytoplasm (By similarity): O74933 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 54844.23 |
| 構造登録者 | Miki, K.,Maruyama, D.,Nishitani, Y.,Nonaka, T.,Kita, A. (登録日: 2007-03-30, 公開日: 2007-05-22, 最終更新日: 2023-10-25) |
| 主引用文献 | Maruyama, D.,Nishitani, Y.,Nonaka, T.,Kita, A.,Fukami, T.A.,Mio, T.,Yamada-Okabe, H.,Yamada-Okabe, T.,Miki, K. Crystal Structure of Uridine-diphospho-N-acetylglucosamine Pyrophosphorylase from Candida albicans and Catalytic Reaction Mechanism J.Biol.Chem., 282:17221-17230, 2007 Cited by PubMed Abstract: Uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc) is a precursor of the bacterial and fungal cell wall. It is also used in a component of N-linked glycosylation and the glycosylphosphoinositol anchor of eukaryotic proteins. It is synthesized from N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and uridine-5'-triphosphate (UTP) by UDP-GlcNAc pyrophosphorylase (UAP). This is an S(N)2 reaction; the non-esterified oxygen atom of the GlcNAc-1-P phosphate group attacks the alpha-phosphate group of UTP. We determined crystal structures of UAP from Candida albicans (CaUAP1) without any ligands and also complexed with its substrate or with its product. The series of structures in different forms shows the induced fit movements of CaUAP1. Three loops approaching the ligand molecule close the active site when ligand is bound. In addition, Lys-421, instead of the metal ion in prokaryotic UAPs, is coordinated by both phosphate groups of UDP-Glc-NAc and acts as a cofactor. However, a magnesium ion enhances the enzymatic activity of CaUAP1, and thus we propose that the magnesium ion increases the affinity between UTP and the enzyme by coordinating to the alpha- and gamma-phosphate group of UTP. PubMed: 17392279DOI: 10.1074/jbc.M611873200 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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