Detailed Information on Publication Record
2011
Complementation of 3D structure of delta subunit of RNA polymerase from Bacillus subtilis with description of internal motions in terms of reduced spectral density mapping
KADEŘÁVEK, Pavel, Carl DIEHL, Veronika PAPOUŠKOVÁ, Hana ŠANDEROVÁ, Petr PADRTA et. al.Basic information
Original name
Complementation of 3D structure of delta subunit of RNA polymerase from Bacillus subtilis with description of internal motions in terms of reduced spectral density mapping
Authors
KADEŘÁVEK, Pavel (203 Czech Republic, guarantor, belonging to the institution), Carl DIEHL (752 Sweden), Veronika PAPOUŠKOVÁ (203 Czech Republic, belonging to the institution), Hana ŠANDEROVÁ (203 Czech Republic), Petr PADRTA (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution), Libor KRÁSNÝ (203 Czech Republic), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution) and Mikael AKKE (752 Sweden)
Edition
MATERIALS STRUCTURE, 2011, 1211-5894
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
RIV identification code
RIV/00216224:14740/11:00057189
Organization unit
Central European Institute of Technology
Keywords in English
NMR; delta subunit; RNA polymerase; spectral density function
Tags
Reviewed
Změněno: 16/4/2013 11:03, Olga Křížová
Abstract
V originále
RNA polymerases of Gram positive and Gram negative bacteria differ. The subunit composition in Gram positive bacteria includes two additional subunits. One of them is denoted delta-subunit. The structure of delta-subunit from Bacillus subtilis has been solved recently using methods of solution NMR [1] (PDB ID = 2KRC). Here, we extend the information about the structure by the basic characterization of its dynamics studied at two temperatures. The standard relaxation experiments (R1, R2, ssNOE) were performed and data were analyzed using reduced spectral density mapping as the most straightforward approach. The analysis reveals flexible residues in the central part of the sequence. It confirms expected independent stochastic movements in the C-terminal part of the molecule. Results also yield an evidence of a slow conformational exchange of several residues in the well-structured region of the protein.
Links
FRVS/1851/2010, interní kód MU |
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GA204/09/0583, research and development project |
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GD301/09/H004, research and development project |
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LC06030, research and development project |
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MSM0021622413, plan (intention) |
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