Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica Section D-Biological Crystallography

ISSN

0907-4449

e-ISSN

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Svazek periodika

70

Číslo periodika v rámci svazku

APR 2014

Stát vydavatele periodika

DK - Dánské království

Počet stran výsledku

15

Strana od-do

943-957

Kód UT WoS článku

000333756700004

EID výsledku v databázi Scopus

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