Detailed Information on Publication Record
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.Basic information
Original name
Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs
Name in Czech
Struktura N-terminální domény delta podjednotky RNA polymerasy z Bacilla subtila a její klasifikace na základě strukturních homologů
Authors
MOTÁČKOVÁ, Veronika (203 Czech Republic, belonging to the institution), Hana ŠANDEROVÁ (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Petr PADRTA (203 Czech Republic, belonging to the institution), Alžběta ŠVENKOVÁ (203 Czech Republic), Jana KORELUSOVÁ (203 Czech Republic), Jiří JONÁK (203 Czech Republic), Libor KRÁSNÝ (203 Czech Republic) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution)
Edition
Proteins: Structure, Function, and Bioinformatics, USA, John Wiley and Sons, 2010, 0887-3585
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 2.813
RIV identification code
RIV/00216224:14310/10:00043931
Organization unit
Faculty of Science
UT WoS
000277302300018
Keywords in English
RNA polymerase; delta subunit; gram positive bacteria; nuclear magnetic resonance; structural homologues
Tags
International impact, Reviewed
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.
In Czech
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.
Links
| GA204/09/0583, research and development project |
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| LC06030, research and development project |
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| MSM0021622413, plan (intention) |
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