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
| Autoři | |
|---|---|
| Rok publikování | 2011 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | MATERIALS STRUCTURE |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | http://www.xray.cz/ms/bul2011-1.htm |
| Obor | Biochemie |
| Klíčová slova | NMR; delta subunit; RNA polymerase; spectral density function |
| Popis | 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. |
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