2010
Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs
MOTÁČKOVÁ, Veronika, Hana ŠANDEROVÁ, Lukáš ŽÍDEK, Jiří NOVÁČEK, Petr PADRTA et. al.Základní údaje
Originální název
Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs
Název česky
Struktura N-terminální domény delta podjednotky RNA polymerasy z Bacilla subtila a její klasifikace na základě strukturních homologů
Autoři
MOTÁČKOVÁ, Veronika (203 Česká republika, domácí), Hana ŠANDEROVÁ (203 Česká republika), Lukáš ŽÍDEK (203 Česká republika, garant, domácí), Jiří NOVÁČEK (203 Česká republika, domácí), Petr PADRTA (203 Česká republika, domácí), Alžběta ŠVENKOVÁ (203 Česká republika), Jana KORELUSOVÁ (203 Česká republika), Jiří JONÁK (203 Česká republika), Libor KRÁSNÝ (203 Česká republika) a Vladimír SKLENÁŘ (203 Česká republika, domácí)
Vydání
Proteins: Structure, Function, and Bioinformatics, USA, John Wiley and Sons, 2010, 0887-3585
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 2.813
Kód RIV
RIV/00216224:14310/10:00043931
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000277302300018
Klíčová slova anglicky
RNA polymerase; delta subunit; gram positive bacteria; nuclear magnetic resonance; structural homologues
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 2. 2. 2012 17:31, Mgr. Veronika Papoušková, Ph.D.
V originále
RNA polymerase is an essential multisubunit enzyme responsible for transcription of genetic information from DNA into RNA. The RNA polymerase from Bacillus subtilis differs from its analogue from gram-negative bacteria in a presence of two additional subunits, omega1 and delta. Their role in the transcription machinery is still not clear. In this study, we focused on the N-terminal part of delta subunit to reveal its structure. The sample was prepared using a standard protocol of overexpression in the E.coli system to produce a 15N,13C-uniformly labeled sample. A standard set of spectra was measured on a 600MHz spectrometer. The distance restrains were extracted and assigned from NOESY spectra. The additional RDC restraints and anisotropic contributions to the 13C chemical shifts were used in the final refinement. The quality of the calculated structures were checked. The determined structure was identified based on structure homology with some proteins from the Forkhead DNA-binding domain SCOP family.
Česky
RNA polymerase is an essential multisubunit enzyme responsible for transcription of genetic information from DNA into RNA. The RNA polymerase from Bacillus subtilis differs from its analogue from gram-negative bacteria in a presence of two additional subunits, omega1 and delta. Their role in the transcription machinery is still not clear. In this study, we focused on the N-terminal part of delta subunit to reveal its structure. The sample was prepared using a standard protocol of overexpression in the E.coli system to produce a 15N,13C-uniformly labeled sample. A standard set of spectra was measured on a 600MHz spectrometer. The distance restrains were extracted and assigned from NOESY spectra. The additional RDC restraints and anisotropic contributions to the 13C chemical shifts were used in the final refinement. The quality of the calculated structures were checked. The determined structure was identified based on structure homology with some proteins from the Forkhead DNA-binding domain SCOP family.
Návaznosti
| GA204/09/0583, projekt VaV |
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| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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