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Crystallographic investigation of the cooperative interaction between trimethoprim, reduced cofactor and dihydrofolate reductase.

Abstract:

The structure of the complex between E. coli (RT500) form I dihydrofolate reductase, the antibacterial trimethoprim and NADPH has been determined by X-ray crystallography. The inhibitor and cofactor are in mutual contact. A flexible chain segment which includes Met 20 is in contact with the inhibitor in the presence of NADPH, but more distant in its absence. By contrast, the inhibitor conformation is little changed with NADPH present. We discuss these observations with regard to the mutually ...

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Publication status:
Published

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Authors


Champness, JN More by this author
Stammers, DK More by this author
Beddell, CR More by this author
Journal:
FEBS letters
Volume:
199
Issue:
1
Pages:
61-67
Publication date:
1986-04-05
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
URN:
uuid:bed9946f-4052-48f0-bd37-01ed86965e17
Source identifiers:
72659
Local pid:
pubs:72659

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