1ofn: Difference between revisions

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[[Image:1ofn.jpg|left|200px]]
{{Seed}}
[[Image:1ofn.png|left|200px]]


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{{STRUCTURE_1ofn|  PDB=1ofn  |  SCENE=  }}  
{{STRUCTURE_1ofn|  PDB=1ofn  |  SCENE=  }}  


'''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.'''
===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==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_12077451}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12077451}}


==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Vancomycin group antibiotic]]
[[Category: Vancomycin group antibiotic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:22:22 2008''

Revision as of 00:22, 29 July 2008

File:1ofn.png

Template:STRUCTURE 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.

Template:ABSTRACT PUBMED 12077451

About this Structure

1OFN is a Single protein structure of sequence from Amycolatopsis orientalis. 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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