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Please use this identifier to cite or link to this item: http://hdl.handle.net/10023/1642
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Title: The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism
Authors: Kowatz, Thomas
Morrison, James P.
Tanner, Martin E.
Naismith, Jim
Keywords: LPS biosynthesis
Hydride transfer
Keto sugar
Carbohydrate
SDR enzymes
Short-chain dehydrogenases/reductases
Udp-galactose 4-epimerase
D-mannoheptose 6-epimerase
Escherichia-coli
RFAD gene
Binding
Biosynthesis
Catalysis
Pathway
QD Chemistry
Issue Date: Jul-2010
Citation: Kowatz , T , Morrison , J P , Tanner , M E & Naismith , J 2010 , ' The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism ' Protein Science , vol 19 , no. 7 , pp. 1337-1343 .
Abstract: Bacteria synthesize a wide array of unusual carbohydrate molecules, which they use in a variety of ways. The carbohydrate L-glycero-D-manno-heptose is an important component of lipopolysaccharide and is synthesized in a complex series of enzymatic steps. One step involves the epimerization at the C6 '' position converting ADP-D-glycero-D-manno-heptose into ADP-L-glycero-D-manno-heptose. The enzyme responsible is a member of the short chain dehydrogenase superfamily, known as ADP-L-glycero-D-manno-heptose 6-epimerase (AGME). The structure of the enzyme was known but the arrangement of the catalytic site with respect to the substrate is unclear. We now report the structure of AGME bound to a substrate mimic, ADP-beta-D-mannose, which has the same stereochemical configuration as the substrate. The complex identifies the key residues and allows mechanistic insight into this novel enzyme.
Version: Publisher PDF
Description: Supported by Wellcome Trust grant 081862/Z/06/Z
Status: Peer reviewed
URI: http://hdl.handle.net/10023/1642
DOI: http://dx.doi.org/10.1002/pro.410
ISSN: 1469-896X
Type: Journal article
Rights: (c)2010 The Protein Society
Appears in Collections:University of St Andrews Research
Chemistry Research
Biomedical Sciences Research Complex (BSRC) Research



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