1LOS

crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP

1LOS の概要

• エントリーDOI: 10.2210/pdb1los/pdb
• 関連するPDBエントリー: 1LOL 1LOQ 1LOR 1LP6
• 分子名称: orotidine monophosphate decarboxylase, 6-AZA URIDINE 5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: tim barrel, lyase
• 由来する生物種: Methanothermobacter thermautotrophicus str. Delta H
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 99169.61

構造登録者

Wu, N.,Pai, E.F. (登録日: 2002-05-06, 公開日: 2002-08-07, 最終更新日: 2024-02-14)

主引用文献

Wu, N.,Pai, E.F.
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.
J.Biol.Chem., 277:28080-28087, 2002

PubMed Abstract: The crystal structures of the enzyme orotidine-5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with its product UMP and the inhibitors 6-hydroxyuridine 5'-phosphate (BMP), XMP, and CMP are reported. A mutant version of the protein, in which four residues of the flexible phosphate-binding loop (180)Gly-Gly(190) were removed and Arg(203) was replaced by alanine, was also analyzed. The XMP and CMP complexes reveal a ligand-binding mode that is distinct from the one identified previously with the aromatic rings located outside the binding pocket. A potential pathway for ligand binding is discussed.

PubMed: 12011084
DOI: 10.1074/jbc.M202362200

実験手法

X-RAY DIFFRACTION (1.9 Å)