3C2P

X-ray crystal structure of the N4 mini-vRNAP P1 promoter complex

3C2P の概要

• エントリーDOI: 10.2210/pdb3c2p/pdb
• 関連するPDBエントリー: 3C3L 3C42 3C46 3C47
• 分子名称: P1 Promoter DNA, Virion RNA polymerase (3 entities in total)
• 機能のキーワード: protein-dna complex, nucleotidyltransferase, promoter binary complex, dna-hairpin, virion rna polymerase, transferase-dna complex, transferase/dna
• 由来する生物種: Bacteriophage N4
• 細胞内の位置: Virion : Q859P9
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 266339.72

構造登録者

Gleghorn, M.L.,Murakami, K.S. (登録日: 2008-01-25, 公開日: 2008-12-09, 最終更新日: 2024-02-21)

主引用文献

Gleghorn, M.L.,Davydova, E.K.,Rothman-Denes, L.B.,Murakami, K.S.
Structural basis for DNA-hairpin promoter recognition by the bacteriophage N4 virion RNA polymerase.
Mol.Cell, 32:707-717, 2008

PubMed Abstract: Coliphage N4 virion-encapsidated RNA polymerase (vRNAP) is a member of the phage T7-like single-subunit RNA polymerase (RNAP) family. Its central domain (mini-vRNAP) contains all RNAP functions of the full-length vRNAP, which recognizes a 5 to 7 base pair stem and 3 nucleotide loop hairpin DNA promoter. Here, we report the X-ray crystal structures of mini-vRNAP bound to promoters. Mini-vRNAP uses four structural motifs to recognize DNA sequences at the hairpin loop and stem and to unwind DNA. Despite their low sequence similarity, three out of four motifs are shared with T7 RNAP that recognizes a double-stranded DNA promoter. The binary complex structure and results of engineered disulfide linkage experiments reveal that the plug and motif B loop, which block the access of template DNA to the active site in the apo-form mini-vRNAP, undergo a large-scale conformational change upon promoter binding, explaining the restricted promoter specificity that is critical for N4 phage early transcription.

PubMed: 19061645
DOI: 10.1016/j.molcel.2008.11.010

実験手法

X-RAY DIFFRACTION (2 Å)