3GZ8

Cocrystal structure of NUDIX domain of Shewanella oneidensis NrtR complexed with ADP ribose

3GZ8 の概要

• エントリーDOI: 10.2210/pdb3gz8/pdb
• 関連するPDBエントリー: 3GZ5 3GZ6
• 分子名称: MutT/nudix family protein, ADENOSINE-5-DIPHOSPHORIBOSE (3 entities in total)
• 機能のキーワード: dna binding protein, nudix domain, whth domain
• 由来する生物種: Shewanella oneidensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75693.17

構造登録者

Huang, N.,Zhang, H. (登録日: 2009-04-06, 公開日: 2009-06-09, 最終更新日: 2023-09-06)

主引用文献

Huang, N.,De Ingeniis, J.,Galeazzi, L.,Mancini, C.,Korostelev, Y.D.,Rakhmaninova, A.B.,Gelfand, M.S.,Rodionov, D.A.,Raffaelli, N.,Zhang, H.
Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism
Structure, 17:939-951, 2009

PubMed Abstract: Besides its function as an essential redox cofactor, nicotinamide adenine dinucleotide (NAD) also serves as a consumable substrate for several reactions with broad impact on many cellular processes. NAD homeostasis appears to be tightly controlled, but the mechanism of its regulation is little understood. Here we demonstrate that a previously predicted bacterial transcriptional regulator, NrtR, represses the transcription of NAD biosynthetic genes in vitro. The NAD metabolite ADP-ribose functions as an activator suppressing NrtR repressor activity. The presence of high ADP-ribose levels in the cell is indicative of active NAD turnover in bacteria, which could signal the activation of NAD biosynthetic gene expression via inhibiting the repressor function of NrtR. By comparing the crystal structures of NrtR in complex with DNA and with ADP-ribose, we identified a "Nudix switch" element that likely plays a critical role in the allosteric regulation of DNA binding and repressor function of NrtR.

PubMed: 19604474
DOI: 10.1016/j.str.2009.05.012

実験手法

X-RAY DIFFRACTION (2.43 Å)