1ofn
From Proteopedia
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| - | [[Image:1ofn. | + | [[Image:1ofn.jpg|left|200px]]<br /><applet load="1ofn" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ofn" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ofn, resolution 1.50Å" /> | caption="1ofn, resolution 1.50Å" /> | ||
'''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.'''<br /> | '''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.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1OFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OFN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vancomycin group antibiotic]] | [[Category: vancomycin group antibiotic]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:40:39 2007'' |
Revision as of 15:30, 18 December 2007
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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 GOL 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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