1OFN

Purification, crystallisation and preliminary structural studies of dTDP-4-keto-6-deoxy-glucose-5-epimerase (EvaD) from Amycolatopsis orientalis; the fourth enzyme in the dTDP-L-epivancosamine biosynthetic pathway.

Summary for 1OFN

• Entry DOI: 10.2210/pdb1ofn/pdb
• Descriptor: PCZA361.16, GLYCEROL (3 entities in total)
• Functional Keywords: epimerase, vancomycin group antibiotic, evad, isomerase
• Biological source: AMYCOLATOPSIS ORIENTALIS (STREPTOMYCES)
• Total number of polymer chains: 2
• Total formula weight: 45391.77

Authors

Merkel, A.B.,Naismith, J.H. (deposition date: 2003-04-17, release date: 2004-04-15, Last modification date: 2023-12-13)

Primary citation

Merkel, A.B.,Temple, G.K.,Burkart, M.D.,Losey, H.C.,Beis, K.,Walsh, C.T.,Naismith, J.H.
Purification, Crystallization and Preliminary Structural Studies of Dtdp-4-Keto-6-Deoxy-Glucose-5-Epimerase (Evad) from Amycolatopsis Orientalis, the Fourth Enzyme in the Dtdp-L-Epivancosamine Biosynthetic Pathway.
Acta Crystallogr.,Sect.D, 58:1226-, 2002

PubMed Abstract: The vancomycin class of antibiotics is regarded as the last line of defence against Gram-positive bacteria. The compounds used clinically are very complex organic molecules and are made by fermentation. The biosynthesis of these is complex and fascinating. Its study holds out the prospect of utilizing genetic engineering of the enzymes in the pathway in order to produce novel vancomycin analogues. In part, this requires detailed structural insight into substrate specificity as well as the enzyme mechanism. The crystallization of one of the enzymes in the chloroeremomycin biosynthetic pathway (a member of the vancomycin family), dTDP-3-amino-4-keto 2,3,6-trideoxy-3-C-methyl-glucose-5-epimerase (EvaD) from Amycolatopsis orientalis, is reported here. The protein is fourth in the pathway which makes a carbohydrate essential for the activity of chloroeremomycin. The crystals of EvaD diffract to 1.5 A and have unit-cell parameters a = 98.6, b = 72.0, c = 57.1 A with space group P2(1)2(1)2. Data to this resolution were collected at the European Synchrotron Radiation Facility.

PubMed: 12077451
DOI: 10.1107/S0907444902007382

Experimental method

X-RAY DIFFRACTION (1.5 Å)