1PEA

AMIDE RECEPTOR/NEGATIVE REGULATOR OF THE AMIDASE OPERON OF PSEUDOMONAS AERUGINOSA (AMIC) COMPLEXED WITH ACETAMIDE

1PEA の概要

• エントリーDOI: 10.2210/pdb1pea/pdb
• 分子名称: AMIDASE OPERON, ACETAMIDE (3 entities in total)
• 機能のキーワード: gene regulator, receptor, binding protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43019.10

構造登録者

Pearl, L.H.,O'Hara, B.P. (登録日: 1995-11-16, 公開日: 1996-04-03, 最終更新日: 2024-02-14)

主引用文献

Pearl, L.,O'Hara, B.,Drew, R.,Wilson, S.
Crystal structure of AmiC: the controller of transcription antitermination in the amidase operon of Pseudomonas aeruginosa.
EMBO J., 13:5810-5817, 1994

PubMed Abstract: The crystal structure for the negative regulator (AmiC) of the amidase operon from Pseudomonas aeruginosa has been solved at a resolution of 2.1 A. AmiC is the amide sensor protein in the amidase operon and regulates the activity of the transcription antitermination factor AmiR, which in turn regulates amidase expression. The AmiC structure consists of two domains with an alternating beta-alpha-beta topology. The two domains are separated by a central cleft and the amide binding site is positioned in this cleft at the interface of the domains. The overall fold for AmiC is extremely similar to that for the leucine-isoleucine-valine binding protein (LivJ) of Escherichia coli despite only 17% sequence identity, however, the two domains of AmiC are substantially closed compared with LivJ. The closed structure of AmiC is stabilized significantly by the bound acetamide, suggesting a molecular mechanism for the process of amide induction. The amide binding site is extremely specific for acetamide and would not allow a closed conformation in the presence of the anti-inducer molecule butyramide.

PubMed: 7813419

実験手法

X-RAY DIFFRACTION (2.1 Å)