CRYSTALLIZATION OF ESCHERICHIA-COLI ENOYL REDUCTASE AND ITS COMPLEX WITH DIAZABORINE

Citation
C. Baldock et al., CRYSTALLIZATION OF ESCHERICHIA-COLI ENOYL REDUCTASE AND ITS COMPLEX WITH DIAZABORINE, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1181-1184
Citations number
17
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
ISSN journal
0907-4449
Volume
52
Year of publication
1996
Part
6
Pages
1181 - 1184
Database
ISI
SICI code
0907-4449(1996)52:<1181:COEERA>2.0.ZU;2-D
Abstract
Recent work has shown that the NADH-dependent enoyl acyl carrier prote in reductase from Escherichia coli is the target for diazaborine, an a ntibacterial agent. This enzyme has been crystallized by the hanging-d rop method of vapour diffusion complexed with NAD(+) and in the presen ce and absence of a thieno diazaborine. The crystals grown in the abse nce of diazaborine (form A) are in the space group P2(1) with unit-cel l dimensions a = 74.0, b = 81.2, c = 79.0 Angstrom and beta = 92.9 deg rees, and with a tetramer in the asymmetric unit, whilst those grown i n the presence of diazaborine (form B) are in the space group P6(1)22 (or P6(5)22) with unit-cell dimensions a = b = 80.9 and c = 328.3 Angs trom, and with a dimer in the asymmetric unit. The structure determina tion of this enzyme in the presence of diazaborine will provide inform ation on the nature of the drug binding site and contribute to a progr amme of rational drug design.