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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F14%3A00435764%21RIV15-AV0-61388971
rdf:type
skos:Concept n17:Vysledek
dcterms: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 results show that the Y9F and F117G mutants are almost non-functional, while the Y17F mutant has almost half of the wild-type activity. In combination with the docking studies, these results suggest that Tyr9 and Phe117 are likely to help to position the substrate for the methyl-transfer reaction and that Tyr9 may also facilitate the reaction by removing an H+ ion. Tyr17, on the other hand, seems to operate by helping to stabilize the SAM cofactor. 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 results show that the Y9F and F117G mutants are almost non-functional, while the Y17F mutant has almost half of the wild-type activity. In combination with the docking studies, these results suggest that Tyr9 and Phe117 are likely to help to position the substrate for the methyl-transfer reaction and that Tyr9 may also facilitate the reaction by removing an H+ ion. Tyr17, on the other hand, seems to operate by helping to stabilize the SAM cofactor.
dcterms:title
Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis
skos:prefLabel
Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis
skos:notation
RIV/61388971:_____/14:00435764!RIV15-AV0-61388971
n3:aktivita
n4:I n4:P
n3:aktivity
I, P(ED1.1.00/02.0109), P(EE2.3.30.0003)
n3:cisloPeriodika
APR 2014
n3:dodaniDat
n12:2015
n3:domaciTvurceVysledku
n11:2389924 n11:5649854 n11:2857693 n11:6327664
n3:druhVysledku
n10:J
n3:duvernostUdaju
n18:S
n3:entitaPredkladatele
n15:predkladatel
n3:idSjednocenehoVysledku
47907
n3:idVysledku
RIV/61388971:_____/14:00435764
n3:jazykVysledku
n9:eng
n3:klicovaSlova
CATECHOL-O-METHYLTRANSFERASE; SN2-LIKE TRANSITION-STATE; CRYSTAL-STRUCTURES
n3:klicoveSlovo
n6:CRYSTAL-STRUCTURES n6:SN2-LIKE%20TRANSITION-STATE n6:CATECHOL-O-METHYLTRANSFERASE
n3:kodStatuVydavatele
DK - Dánské království
n3:kontrolniKodProRIV
[E1F05A2B9C6B]
n3:nazevZdroje
Acta Crystallographica Section D-Biological Crystallography
n3:obor
n13:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
8
n3:projekt
n14:EE2.3.30.0003 n14:ED1.1.00%2F02.0109
n3:rokUplatneniVysledku
n12:2014
n3:svazekPeriodika
70
n3:tvurceVysledku
Koštan, J. Janata, Jiří Kutejová, Eva Najmanová, Lucie Ondrovičová, G. Kameník, Zdeněk Bauer, J. Pevala, V.
n3:wos
000333756700004
s:issn
0907-4449
s:numberOfPages
15
n7:doi
10.1107/S139900471303397X