1EIX

STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP

1EIX の概要

• エントリーDOI: 10.2210/pdb1eix/pdb
• 分子名称: OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE, 1-(5'-PHOSPHO-BETA-D-RIBOFURANOSYL)BARBITURIC ACID (3 entities in total)
• 機能のキーワード: alpha-beta-barrel, protein-inhibitor complex, homodimer, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 106873.62

構造登録者

Harris, P.,Poulsen, J.C.N.,Jensen, K.F.,Larsen, S. (登録日: 2000-02-29, 公開日: 2000-03-15, 最終更新日: 2024-03-13)

主引用文献

Harris, P.,Poulsen, J.C.N.,Jensen, K.F.,Larsen, S.
Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
Biochemistry, 39:4217-4224, 2000

PubMed Abstract: Orotidine 5'-monophosphate decarboxylase (ODCase) catalyzes the decarboxylation of orotidine 5'-monophosphate, the last step in the de novo synthesis of uridine 5'-monophosphate. ODCase is a very proficient enzyme [Radzicka, A., and Wolfenden, R. (1995) Science 267, 90-93], enhancing the reaction rate by a factor of 10(17). This proficiency has been enigmatic, since it is achieved without metal ions or cofactors. Here we present a 2.5 A resolution structure of ODCase complexed with the inhibitor 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid. It shows a closely packed dimer composed of two alpha/beta-barrels with two shared active sites. The orientation of the orotate moiety of the substrate is unambiguously deduced from the structure, and previously proposed catalytic mechanisms involving protonation of O2 or O4 can be ruled out. The proximity of the OMP carboxylate group with Asp71 appears to be instrumental for the decarboxylation of OMP, either through charge repulsion or through the formation of a very short O.H.O hydrogen bond between the two carboxylate groups.

PubMed: 10757968
DOI: 10.1021/bi992952r

実験手法

X-RAY DIFFRACTION (2.5 Å)