3GZ8

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

Summary for 3GZ8

• Entry DOI: 10.2210/pdb3gz8/pdb
• Related: 3GZ5 3GZ6
• Descriptor: MutT/nudix family protein, ADENOSINE-5-DIPHOSPHORIBOSE (3 entities in total)
• Functional Keywords: dna binding protein, nudix domain, whth domain
• Biological source: Shewanella oneidensis
• Total number of polymer chains: 4
• Total formula weight: 75693.17

Authors

Huang, N.,Zhang, H. (deposition date: 2009-04-06, release date: 2009-06-09, Last modification date: 2023-09-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.43 Å)