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1TLH

T4 AsiA bound to sigma70 region 4

Summary for 1TLH
Entry DOI10.2210/pdb1tlh/pdb
Related1TKV 1TL6
Descriptor10 kDa anti-sigma factor, RNA polymerase sigma factor rpoD (2 entities in total)
Functional Keywordsanti-sigma, sigma70, rna polymerase, transcription
Biological sourceEnterobacteria phage T4
More
Cellular locationCytoplasm (Potential): P00579
Total number of polymer chains2
Total formula weight19924.58
Authors
Lambert, L.J.,Wei, Y.,Schirf, V.,Demeler, B.,Werner, M.H. (deposition date: 2004-06-09, release date: 2004-11-23, Last modification date: 2024-05-01)
Primary citationLambert, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237735

数据于2025-06-18公开中

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