1TTY

Solution structure of sigma A region 4 from Thermotoga maritima

Summary for 1TTY

• Entry DOI: 10.2210/pdb1tty/pdb
• Descriptor: RNA polymerase sigma factor rpoD (1 entity in total)
• Functional Keywords: sigma factor, rna polymerase, helix-turn-helix, transcription
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 10384.33

Authors

Lambert, L.J.,Wei, Y.,Schirf, V.,Demeler, B.,Werner, M.H. (deposition date: 2004-06-23, release date: 2004-11-23, Last modification date: 2024-05-22)

Primary citation

Lambert, L.J.,Wei, Y.,Schirf, V.,Demeler, B.,Werner, M.H.
T4 AsiA blocks DNA recognition by remodeling sigma(70) region 4
Embo J., 23:2952-2962, 2004

PubMed Abstract: Bacteriophage T4 AsiA is a versatile transcription factor capable of inhibiting host gene expression as an 'anti-sigma' factor while simultaneously promoting gene-specific expression of T4 middle genes in conjunction with T4 MotA. To accomplish this task, AsiA engages conserved region 4 of Eschericia coli sigma70, blocking recognition of most host promoters by sequestering the DNA-binding surface at the AsiA/sigma70 interface. The three-dimensional structure of an AsiA/region 4 complex reveals that the C-terminal alpha helix of region 4 is unstructured, while four other helices adopt a completely different conformation relative to the canonical structure of unbound region 4. That AsiA induces, rather than merely stabilizes, this rearrangement can be realized by comparison to the homologous structures of region 4 solved in a variety of contexts, including the structure of Thermotoga maritima sigmaA region 4 described herein. AsiA simultaneously occupies the surface of region 4 that ordinarily contacts core RNA polymerase (RNAP), suggesting that an AsiA-bound sigma70 may also undergo conformational changes in the context of the RNAP holoenzyme.

PubMed: 15257291
DOI: 10.1038/sj.emboj.7600312

Experimental method

SOLUTION NMR