Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F14%3A00435764" target="_blank" >RIV/61388971:_____/14:00435764 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1107/S139900471303397X" target="_blank" >http://dx.doi.org/10.1107/S139900471303397X</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S139900471303397X" target="_blank" >10.1107/S139900471303397X</a>
Alternative languages
Result language
angličtina
Original language name
Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis
Original language description
The S-adenosyl-L-methionine (SAM)-dependent methyltransferase CcbJ from Streptomyces caelestis catalyzes one of the final steps in the biosynthesis of the antibiotic celesticetin, methylation of the N atom of its proline moiety, which greatly enhances the activity of the antibiotic. Since several celesticetin variants exist, this enzyme may be able to act on a variety of substrates. The structures of CcbJ determined by MAD phasing at 3.0 angstrom resolution, its native form at 2.7 angstrom resolution and its complex with S-adenosyl-l-homocysteine (SAH) at 2.9 angstrom resolution are reported here. Based on these structures, three point mutants, Y9F, Y17F and F117G, were prepared in order to study its behaviour as well as docking simulations of both CcbJ-SAM-substrate and CcbJ-SAH-product complexes. The structures show that CcbJ is a class I SAM-dependent methyltransferase with a wide active site, thereby suggesting that it may accommodate a number of different substrates. The mutation
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section D-Biological Crystallography
ISSN
0907-4449
e-ISSN
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Volume of the periodical
70
Issue of the periodical within the volume
APR 2014
Country of publishing house
DK - DENMARK
Number of pages
15
Pages from-to
943-957
UT code for WoS article
000333756700004
EID of the result in the Scopus database
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