1oi6

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{{STRUCTURE_1oi6| PDB=1oi6 | SCENE= }}
{{STRUCTURE_1oi6| PDB=1oi6 | SCENE= }}
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'''STRUCTURE DETERMINATION OF THE TMP-COMPLEX OF EVAD'''
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===STRUCTURE DETERMINATION OF THE TMP-COMPLEX OF EVAD===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15159413}}
==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 10:53:52 2008''

Revision as of 07:53, 29 July 2008

Image:1oi6.png

Template:STRUCTURE 1oi6

STRUCTURE DETERMINATION OF THE TMP-COMPLEX OF EVAD

Template:ABSTRACT PUBMED 15159413

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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