1oi6
From Proteopedia
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| - | [[Image:1oi6.gif|left|200px]] | + | [[Image:1oi6.gif|left|200px]] |
| - | + | ||
| - | '''STRUCTURE DETERMINATION OF THE TMP-COMPLEX OF EVAD''' | + | {{Structure |
| + | |PDB= 1oi6 |SIZE=350|CAPTION= <scene name='initialview01'>1oi6</scene>, resolution 1.40Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=TMP:THYMIDINE-5'-PHOSPHATE'>TMP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE DETERMINATION OF THE TMP-COMPLEX OF EVAD''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OI6 is a [ | + | 1OI6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OI6 OCA]. |
==Reference== | ==Reference== | ||
| - | The position of a key tyrosine in dTDP-4-Keto-6-deoxy-D-glucose-5-epimerase (EvaD) alters the substrate profile for this RmlC-like enzyme., Merkel AB, Major LL, Errey JC, Burkart MD, Field RA, Walsh CT, Naismith JH, J Biol Chem. 2004 Jul 30;279(31):32684-91. Epub 2004 May 24. PMID:[http:// | + | The position of a key tyrosine in dTDP-4-Keto-6-deoxy-D-glucose-5-epimerase (EvaD) alters the substrate profile for this RmlC-like enzyme., Merkel AB, Major LL, Errey JC, Burkart MD, Field RA, Walsh CT, Naismith JH, J Biol Chem. 2004 Jul 30;279(31):32684-91. Epub 2004 May 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15159413 15159413] |
[[Category: Amycolatopsis orientalis]] | [[Category: Amycolatopsis orientalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vancomycin group antibiotic]] | [[Category: vancomycin group antibiotic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:14 2008'' |
Revision as of 11:11, 20 March 2008
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| , resolution 1.40Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE DETERMINATION OF THE TMP-COMPLEX OF EVAD
Overview
Vancomycin, the last line of defense antibiotic, depends upon the attachment of the carbohydrate vancosamine to an aglycone skeleton for antibacterial activity. Vancomycin is a naturally occurring secondary metabolite that can be produced by bacterial fermentation. To combat emerging resistance, it has been proposed to genetically engineer bacteria to produce analogues of vancomycin. This requires a detailed understanding of the biochemical steps in the synthesis of vancomycin. Here we report the 1.4 A structure and biochemical characterization of EvaD, an RmlC-like protein that is required for the C-5' epimerization during synthesis of dTDP-epivancosamine. EvaD, although clearly belonging to the RmlC class of enzymes, displays very low activity in the archetypal RmlC reaction (double epimerization of dTDP-6-deoxy-4-keto-D-glucose at C-3' and C-5'). The high resolution structure of EvaD compared with the structures of authentic RmlC enzymes indicates that a subtle change in the enzyme active site repositions a key catalytic Tyr residue. A mutant designed to re-establish the normal position of the Tyr increases the RmlC-like activity of EvaD.
About this Structure
1OI6 is a Single protein structure of sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA.
Reference
The position of a key tyrosine in dTDP-4-Keto-6-deoxy-D-glucose-5-epimerase (EvaD) alters the substrate profile for this RmlC-like enzyme., Merkel AB, Major LL, Errey JC, Burkart MD, Field RA, Walsh CT, Naismith JH, J Biol Chem. 2004 Jul 30;279(31):32684-91. Epub 2004 May 24. PMID:15159413
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