1VIE

STRUCTURE OF DIHYDROFOLATE REDUCTASE

Summary for 1VIE

• Entry DOI: 10.2210/pdb1vie/pdb
• Descriptor: DIHYDROFOLATE REDUCTASE (2 entities in total)
• Functional Keywords: oxidoreductase, nadp, trimethoprim resistance, methotrexate resistance, one-carbon metabolism, plasmid
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 6732.53

Authors

Narayana, N.,Matthews, D.A.,Howell, E.E.,Xuong, N.-H. (deposition date: 1996-10-03, release date: 1997-10-22, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)