2PO4

X-ray crystal structure of polymerase domain of the bacteriophage N4 virion RNA polymerase

2PO4 の概要

• エントリーDOI: 10.2210/pdb2po4/pdb
• 分子名称: Virion RNA polymerase (2 entities in total)
• 機能のキーワード: right hand shape, transferase
• 由来する生物種: Enterobacteria phage N4
• 細胞内の位置: Virion : Q859P9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 121559.70

構造登録者

Murakami, K.S.,Davydova, E.K.,Rothman-Denes, L.B. (登録日: 2007-04-25, 公開日: 2008-04-01, 最終更新日: 2024-02-21)

主引用文献

Murakami, K.S.,Davydova, E.K.,Rothman-Denes, L.B.
X-ray crystal structure of polymerase domain of the bacteriophage N4 virion RNA polymerase
Proc.Natl.Acad.Sci.USA, 15:5046-5051, 2008

PubMed Abstract: Coliphage N4 virion RNA polymerase (vRNAP), which is injected into the host upon infection, transcribes the phage early genes from promoters that have a 5-bp stem-3 nt loop hairpin structure. Here, we describe the 2.0-A resolution x-ray crystal structure of N4 mini-vRNAP, a member of the T7-like, single-unit RNAP family and the minimal component having all RNAP functions of the full-length vRNAP. The structure resembles a "fisted right hand" with Fingers, Palm and Thumb subdomains connected to an N-terminal domain. We established that the specificity loop extending from the Fingers along with W129 of the N-terminal domain play critical roles in hairpin-promoter recognition. A comparison with the structure of the T7 RNAP initiation complex reveals that the pathway of the DNA to the active site is blocked in the apo-form vRNAP, indicating that vRNAP must undergo a large-scale conformational change upon promoter DNA binding and explaining the highly restricted promoter specificity of vRNAP that is essential for phage early transcription.

PubMed: 18362338
DOI: 10.1073/pnas.0712325105

実験手法

X-RAY DIFFRACTION (2 Å)