1LX7

Structure of E. coli uridine phosphorylase at 2.0A

1LX7 の概要

• エントリーDOI: 10.2210/pdb1lx7/pdb
• 関連するPDBエントリー: 1k3f
• 分子名称: uridine phosphorylase (2 entities in total)
• 機能のキーワード: structural genomics, udrpase, p12758, phosphorylase, nucleotide metabolism, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, transferase
• 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: 55128.43

構造登録者

Burling, T.,Buglino, J.A.,Kniewel, R.,Chadna, T.,Beckwith, A.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2002-06-04, 公開日: 2002-06-12, 最終更新日: 2024-10-30)

主引用文献

Burling, F.T.,Kniewel, R.,Buglino, J.A.,Chadha, T.,Beckwith, A.,Lima, C.D.
Structure of Escherichia coli uridine phosphorylase at 2.0 A.
Acta Crystallogr.,Sect.D, 59:73-76, 2003

PubMed Abstract: The 2.0 A crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0 A model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated.

PubMed: 12499542
DOI: 10.1107/S0907444902018929

実験手法

X-RAY DIFFRACTION (2 Å)