1a47
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CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR
OverviewOverview
The product specificity and pH optimum of the thermostable cyclodextrin, glycosyltransferase (CGTase) from Thermoanaerobacterium thermosulfurigenes, EM1 was engineered using a combination of x-ray crystallography and, site-directed mutagenesis. Previously, a crystal soaking experiment with, the Bacillus circulans strain 251 beta-CGTase had revealed a maltononaose, inhibitor bound to the enzyme in an extended conformation. An identical, experiment with the CGTase from T. thermosulfurigenes EM1 resulted in a, 2.6-A resolution x-ray structure of a complex with a maltohexaose, inhibitor, bound in a different conformation. We hypothesize that the new, maltohexaose conformation is related to the enhanced alpha-cyclodextrin, production of the CGTase. The detailed structural information ... [(full description)]
About this StructureAbout this Structure
1A47 is a [Single protein] structure of sequence from [Thermoanaerobacterium thermosulfurigenes] with CA as [ligand]. Active as [Cyclomaltodextrin glucanotransferase], with EC number [2.4.1.19]. Structure known Active Sites: AM1, AM2, AM3, AP1, AP2, AP3, BS3, CA1 and CA2. Full crystallographic information is available from [OCA].
ReferenceReference
Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1., Wind RD, Uitdehaag JC, Buitelaar RM, Dijkstra BW, Dijkhuizen L, J Biol Chem. 1998 Mar 6;273(10):5771-9. PMID:9488711
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