3DZD

Crystal structure of sigma54 activator NTRC4 in the inactive state

3DZD の概要

• エントリーDOI: 10.2210/pdb3dzd/pdb
• 関連するPDBエントリー: 3E7L
• 分子名称: Transcriptional regulator (NtrC family), ADENOSINE-5'-DIPHOSPHATE, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: sigma43 activator, aaa+ atpase, response regulator, transcriptional activator, atp-binding, nucleotide-binding, transcription, transcription regulation, transcription regulator
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84773.42

構造登録者

Batchelor, J.D.,Doucleff, M.,Lee, C.-J.,Matsubara, K.,De Carlo, S.,Heideker, J.,Lamers, M.M.,Pelton, J.G.,Wemmer, D.E. (登録日: 2008-07-29, 公開日: 2008-11-25, 最終更新日: 2024-11-13)

主引用文献

Batchelor, J.D.,Doucleff, M.,Lee, C.J.,Matsubara, K.,De Carlo, S.,Heideker, J.,Lamers, M.H.,Pelton, J.G.,Wemmer, D.E.
Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation.
J.Mol.Biol., 384:1058-1075, 2008

PubMed Abstract: Genetic changes lead gradually to altered protein function, making deduction of the molecular basis for activity from a sequence difficult. Comparative studies provide insights into the functional consequences of specific changes. Here we present structural and biochemical studies of NtrC4, a sigma-54 activator from Aquifex aeolicus, and compare it with NtrC1 (a paralog) and NtrC (a homolog from Salmonella enterica) to provide insight into how a substantial change in regulatory mechanism may have occurred. Activity assays show that assembly of NtrC4's active oligomer is repressed by the N-terminal receiver domain, and that BeF3- addition (mimicking phosphorylation) removes this repression. Observation of assembly without activation for NtrC4 indicates that it is much less strongly repressed than NtrC1. The crystal structure of the unactivated receiver-ATPase domain combination shows a partially disrupted interface. NMR structures of the regulatory domain show that its activation mechanism is very similar to that of NtrC1. The crystal structure of the NtrC4 DNA-binding domain shows that it is dimeric and more similar in structure to NtrC than NtrC1. Electron microscope images of the ATPase-DNA-binding domain combination show formation of oligomeric rings. Sequence alignments provide insights into the distribution of activation mechanisms in this family of proteins.

PubMed: 18955063
DOI: 10.1016/j.jmb.2008.10.024

実験手法

X-RAY DIFFRACTION (2.4 Å)