2C98

Structural basis of the nucleotide driven conformational changes in the AAA domain of transcription activator PspF

2C98 の概要

• エントリーDOI: 10.2210/pdb2c98/pdb
• 関連するPDBエントリー: 2BJV 2BJW 2C96 2C99 2C9C
• 分子名称: PSP OPERON TRANSCRIPTIONAL ACTIVATOR, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: bacterial sigma54 activator, atpase, atp-binding, dna-binding, sensory transduction, transcription regulation, two-component regulatory system
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm (Potential): P37344
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30414.50

構造登録者

Rappas, M.,Schumacher, J.,Niwa, H.,Buck, M.,Zhang, X. (登録日: 2005-12-09, 公開日: 2006-02-01, 最終更新日: 2023-12-13)

主引用文献

Rappas, M.,Schumacher, J.,Niwa, H.,Buck, M.,Zhang, X.
Structural Basis of the Nucleotide Driven Conformational Changes in the Aaa(+) Domain of Transcription Activator Pspf.
J.Mol.Biol., 357:481-, 2006

PubMed Abstract: Bacterial enhancer-binding proteins (EBP) activate transcription by hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter complex. We compare six high resolution structures (<2.1 A) of the AAA(+) domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the atomic details underpinning the origins of the conformational changes occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain respond distinctively to nucleotide binding and hydrolysis, suggesting functional roles during the hydrolysis cycle, which completely agree with those derived from activities of PspF mutated at these positions. We propose a putative atomic switch that is responsible for coupling structural changes in the nucleotide-binding site to the repositioning of the sigma(54)-interacting loops. Striking similarities in nucleotide-specific conformational changes and atomic switch exist between PspF and the large T antigen helicase, suggesting conservation in the origin of those events amongst AAA(+) proteins.

PubMed: 16430918
DOI: 10.1016/J.JMB.2005.12.052

実験手法

X-RAY DIFFRACTION (1.9 Å)