1VIF

STRUCTURE OF DIHYDROFOLATE REDUCTASE

1VIF の概要

• エントリーDOI: 10.2210/pdb1vif/pdb
• 分子名称: DIHYDROFOLATE REDUCTASE, FOLIC ACID (3 entities in total)
• 機能のキーワード: oxidoreductase, nadp, trimethoprim resistance methotrexate resistance, one-carbon metabolism, plasmid
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7173.93

構造登録者

Narayana, N.,Matthews, D.A.,Howell, E.E.,Xuong, N.-H. (登録日: 1996-10-03, 公開日: 1997-10-22, 最終更新日: 2024-05-22)

主引用文献

Narayana, N.,Matthews, D.A.,Howell, E.E.,Nguyen-huu, X.
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site.
Nat.Struct.Biol., 2:1018-1025, 1995

PubMed Abstract: Bacteria expressing R67-plasmid encoded dihydrofolate reductase (R67 DHFR) exhibit high-level resistance to the antibiotic trimethoprim. Native R67 DHFR is a 34,000 M(r) homotetramer which exists in equilibrium with an inactive dimeric form. The structure of native R67 DHFR has now been solved at 1.7 A resolution and is unrelated to that of chromosomal DHFR. Homotetrameric R67 DHFR has an unusual pore, 25 A in length, passing through the middle of the molecule. Two folate molecules bind asymmetrically within the pore indicating that the enzyme's active site consists of symmetry related binding surfaces from all four identical units.

PubMed: 7583655
DOI: 10.1038/nsb1195-1018

実験手法

X-RAY DIFFRACTION (1.8 Å)