1L2U

Orotidine 5'-monophosphate decarboxylase from E. coli

1L2U の概要

• エントリーDOI: 10.2210/pdb1l2u/pdb
• 関連するPDBエントリー: 1EIX 1JJK
• 分子名称: Orotidine 5'-phosphate decarboxylase (2 entities in total)
• 機能のキーワード: beta-alpha-barrel, homodimer, twinned crystals, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52756.45

構造登録者

Harris, P.,Poulsen, J.C.,Jensen, K.F.,Larsen, S. (登録日: 2002-02-25, 公開日: 2002-03-13, 最終更新日: 2023-08-16)

主引用文献

Harris, P.,Poulsen, J.C.,Jensen, K.F.,Larsen, S.
Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase
J.Mol.Biol., 18:1019-1029, 2002

PubMed Abstract: Orotidine 5'-monophosphate decarboxylase (ODCase) catalyses the decarboxylation of orotidine 5'-monophosphate to uridine 5'-monophosphate (UMP). We have earlier determined the structure of ODCase from Escherichia coli complexed with the inhibitor 1-(5'-phospho-beta-d-ribofuranosyl)barbituric acid (BMP); here we present the 2.5 A structure of the uncomplexed apo enzyme, determined from twinned crystals. A structural analysis and comparison of the two structures of the E. coli enzyme show that binding of the inhibitor is accompanied by significant domain movements of approximately 12 degrees around a hinge that crosses the active site. Hence, the ODCase dimer, which contains two active sites, may be divided in three domains: a central domain that is fixed, and two lids which independently move 12 degrees upon binding. Corresponding analyses, presented herein, of the two Saccharomyces cerevisiae ODCase structures (with and without BMP) and the Methanobacterium thermoautotrophicum ODCase structures (with and without 6-aza UMP) show very similar, but somewhat smaller domain movements. The domain movements seem to be initiated by the phosphoryl binding to the enzyme and can explain why the binding of the phosphoryl group is essential for the catalytic function.

PubMed: 12054799
DOI: 10.1016/S0022-2836(02)00200-0

実験手法

X-RAY DIFFRACTION (2.5 Å)