1GRJ

GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI

1GRJ の概要

• エントリーDOI: 10.2210/pdb1grj/pdb
• 分子名称: GREA PROTEIN (2 entities in total)
• 機能のキーワード: transcript elongation factor, transcript cleavage factor, transcription regulation
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17662.93

構造登録者

Darst, S.A.,Stebbins, C.E. (登録日: 1995-05-02, 公開日: 1995-07-10, 最終更新日: 2024-02-07)

主引用文献

Stebbins, C.E.,Borukhov, S.,Orlova, M.,Polyakov, A.,Goldfarb, A.,Darst, S.A.
Crystal structure of the GreA transcript cleavage factor from Escherichia coli.
Nature, 373:636-640, 1995

PubMed Abstract: Transcription elongation factors stimulate the activity of DNA-dependent RNA polymerases by increasing the overall elongation rate and the completion of RNA chains. One group of such factors, which includes Escherichia coli GreA, GreB and eukaryotic SII (TFIIS), acts by inducing hydrolytic cleavage of the transcript within the RNA polymerase, followed by release of the 3'-terminal fragment. Here we report the crystal structure of GreA at 2.2 A resolution. The structure contains an amino-terminal domain consisting of an antiparallel alpha-helical coiled-coil dimer which extends into solution, reminiscent of the coiled coil in seryl-tRNA synthetases. A site near the tip of the coiled-coil 'finger' plays a direct role in the transcript cleavage reaction by contacting the 3'-end of the transcript. The structure exhibits an unusual asymmetric charge distribution which indicates the manner in which GreA interacts with the RNA polymerase elongation complex.

PubMed: 7854424
DOI: 10.1038/373636a0

実験手法

X-RAY DIFFRACTION (2.2 Å)