1ofn
From Proteopedia
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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.
Overview
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.
About this Structure
1OFN is a Single protein structure of sequence from Amycolatopsis orientalis with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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., Merkel AB, Temple GK, Burkart MD, Losey HC, Beis K, Walsh CT, Naismith JH, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1226-8. Epub 2002, Jun 20. PMID:12077451
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