4JKR

Crystal Structure of E. coli RNA Polymerase in complex with ppGpp

4JKR の概要

• エントリーDOI: 10.2210/pdb4jkr/pdb
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA', ... (8 entities in total)
• 機能のキーワード: rna polymerase, transcription regulation, transcription, transferase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm (Potential): P00579
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 927768.68

構造登録者

Zuo, Y.,Wang, Y.,Steitz, T.A. (登録日: 2013-03-11, 公開日: 2013-05-15, 最終更新日: 2024-02-28)

主引用文献

Zuo, Y.,Wang, Y.,Steitz, T.A.
The mechanism of E. coli RNA polymerase regulation by ppGpp is suggested by the structure of their complex.
Mol.Cell, 50:430-436, 2013

PubMed Abstract: Guanosine tetraphosphate (ppGpp) is an alarmone that enables bacteria to adapt to their environment. It has been known for years that ppGpp acts directly on RNA polymerase (RNAP) to alter the rate of transcription, but its exact target site is still under debate. Here we report a crystal structure of Escherichia coli RNAP holoenzyme in complex with ppGpp at 4.5 Å resolution. The structure reveals that ppGpp binds at an interface between the shelf and core modules on the outer surface of RNAP, away from the catalytic center and the nucleic acid binding path. Bound ppGpp connects these two pivotal modules that may restrain the opening of the RNAP cleft. A detailed mechanism of action of ppGpp is proposed in which ppGpp prevents the closure of the active center that is induced by the binding of NTP, which could slow down nucleotide addition cycles and destabilize the initial transcription complexes.

PubMed: 23623685
DOI: 10.1016/j.molcel.2013.03.020

実験手法

X-RAY DIFFRACTION (4.2 Å)