4R7P

Human UDP-glucose pyrophosphorylase isoform 1 in complex with UDP-glucose

4R7P の概要

• エントリーDOI: 10.2210/pdb4r7p/pdb
• 関連するPDBエントリー: 3R2W 3R3I
• 分子名称: UTP--glucose-1-phosphate uridylyltransferase, URIDINE-5'-DIPHOSPHATE-GLUCOSE, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: rossmann-like alpha/beta/alpha sandwich fold, pyrophosphorylase, utp, glc-1-p, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q16851
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 239454.47

構造登録者

Fuehring, J.,Cramer, J.T.,Schneider, J.,Baruch, P.,Gerardy-Schahn, R.,Fedorov, R. (登録日: 2014-08-28, 公開日: 2015-04-22, 最終更新日: 2024-02-28)

主引用文献

Fuhring, J.I.,Cramer, J.T.,Schneider, J.,Baruch, P.,Gerardy-Schahn, R.,Fedorov, R.
A Quaternary Mechanism Enables the Complex Biological Functions of Octameric Human UDP-glucose Pyrophosphorylase, a Key Enzyme in Cell Metabolism.
Sci Rep, 5:9618-9618,

PubMed Abstract: In mammals, UDP-glucose pyrophosphorylase (UGP) is the only enzyme capable of activating glucose-1-phosphate (Glc-1-P) to UDP-glucose (UDP-Glc), a metabolite located at the intersection of virtually all metabolic pathways in the mammalian cell. Despite the essential role of its product, the molecular basis of UGP function is poorly understood. Here we report the crystal structure of human UGP in complex with its product UDP-Glc. Beyond providing first insight into the active site architecture, we describe the substrate binding mode and intermolecular interactions in the octameric enzyme that are crucial to its activity. Importantly, the quaternary mechanism identified for human UGP in this study may be common for oligomeric sugar-activating nucleotidyltransferases. Elucidating such mechanisms is essential for understanding nucleotide sugar metabolism and opens the perspective for the development of drugs that specifically inhibit simpler organized nucleotidyltransferases in pathogens.

PubMed: 25860585
DOI: 10.1038/srep09618

実験手法

X-RAY DIFFRACTION (3.35 Å)