1vif
From Proteopedia
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'''STRUCTURE OF DIHYDROFOLATE REDUCTASE''' | '''STRUCTURE OF DIHYDROFOLATE REDUCTASE''' | ||
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[[Category: Narayana, N.]] | [[Category: Narayana, N.]] | ||
[[Category: Xuong, N H.]] | [[Category: Xuong, N H.]] | ||
| - | [[Category: | + | [[Category: Nadp]] |
| - | [[Category: | + | [[Category: One-carbon metabolism]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Plasmid]] |
| - | [[Category: | + | [[Category: Trimethoprim resistance methotrexate resistance]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:34:02 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:34, 3 May 2008
STRUCTURE OF DIHYDROFOLATE REDUCTASE
Overview
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.
About this Structure
1VIF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site., Narayana N, Matthews DA, Howell EE, Nguyen-huu X, Nat Struct Biol. 1995 Nov;2(11):1018-25. PMID:7583655 Page seeded by OCA on Sat May 3 12:34:02 2008
