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PMID:23662776
| Citation |
'Singh, S, Chang, A, Helmich, KE, Bingman, CA, Wrobel, RL, Beebe, ET, Makino, SI, Aceti, DJ, Dyer, K, Hura, GL, Sunkara, M, Morris, AJ, Phillips, GN Jr and Thorson, JS (2013) Structural and Functional Characterization of CalS11, a TDP-Rhamnose 3'-O-Methyltransferase Involved in Calicheamicin Biosynthesis. ACS Chem. Biol. ' |
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| Abstract |
Sugar methyltransferases (MTs) are an important class of tailoring enzymes that catalyze the transfer of a methyl group from S-adenosyl-l-methionine to sugar-based N-, C- and O-nucleophiles. While sugar N- and C-MTs involved in natural product biosynthesis have been found to act on sugar nucleotide substrates prior to a subsequent glycosyltransferase reaction, corresponding sugar O-methylation reactions studied thus far occur after the glycosyltransfer reaction. Herein we report the first in vitro characterization using (1)H-(13)C-gHSQC with isotopically labeled substrates and the X-ray structure determination at 1.55 Å resolution of the TDP-3'-O-rhamnose-methyltransferase CalS11 from Micromonospora echinospora. This study highlights a unique NMR-based methyltransferase assay, implicates CalS11 to be a metal- and general acid/base-dependent O-methyltransferase, and as a first crystal structure for a TDP-hexose-O-methyltransferase, presents a new template for mechanistic studies and/or engineering. |
| Links |
PubMed Online version:10.1021/cb400068k |
| Keywords |
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| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0008171: O-methyltransferase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0008171: |
ECO:0000314: |
CalS11 is a sugar O-methyltransferase from calicheamicin gene cluster from the organism Micromonospora echinospora.Its structure was discovered in this paper, as seen in Figures 4-7. |
complete | |||||
| GO:0008171: O-methyltransferase activity |
ECO:0000314: |
F |
The function of CalG4 was determined in this paper via NMR spectroscopy as shown in Figure 3. |
complete | ||||
See also
References
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