2M4K

Solution structure of the delta subunit of RNA polymerase from Bacillus subtilis

Summary for 2M4K

• Entry DOI: 10.2210/pdb2m4k/pdb
• NMR Information: BMRB: 16912
• Descriptor: DNA-directed RNA polymerase subunit delta (1 entity in total)
• Functional Keywords: delta subunit, rna polymerase, transferase
• Biological source: Bacillus subtilis subsp. subtilis
• Total number of polymer chains: 1
• Total formula weight: 20286.69

Authors

Papouskova, V.,Novacek, J.,Kaderavek, P.,Zidek, L.,Rabatinova, A.,Sanderova, H.,Krasny, L.,Sklenar, V. (deposition date: 2013-02-07, release date: 2013-10-09, Last modification date: 2024-05-15)

Primary citation

Papouskova, V.,Kaderavek, P.,Otrusinova, O.,Rabatinova, A.,Sanderova, H.,Novacek, J.,Krasny, L.,Sklenar, V.,Zidek, L.
Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis.
Chembiochem, 14:1772-1779, 2013

PubMed Abstract: The partially disordered δ subunit of RNA polymerase was studied by various NMR techniques. The structure of the well-folded N-terminal domain was determined based on inter-proton distances in NOESY spectra. The obtained structural model was compared to the previously determined structure of a truncated construct (lacking the C-terminal domain). Only marginal differences were identified, thus indicating that the first structural model was not significantly compromised by the absence of the C-terminal domain. Various (15) N relaxation experiments were employed to describe the flexibility of both domains. The relaxation data revealed that the C-terminal domain is more flexible, but its flexibility is not uniform. By using paramagnetic labels, transient contacts of the C-terminal tail with the N-terminal domain and with itself were identified. A propensity of the C-terminal domain to form β-type structures was obtained by chemical shift analysis. Comparison with the paramagnetic relaxation enhancement indicated a well-balanced interplay of repulsive and attractive electrostatic interactions governing the conformational behavior of the C-terminal domain. The results showed that the δ subunit consists of a well-ordered N-terminal domain and a flexible C-terminal domain that exhibits a complex hierarchy of partial ordering.

PubMed: 23868186
DOI: 10.1002/cbic.201300226

Experimental method

SOLUTION NMR