CryoEM structure of the trifunctional NAD biosynthesis/regulator protein NadR in complex with NADCryoEM structure of the trifunctional NAD biosynthesis/regulator protein NadR in complex with NAD

Structural highlights

8x7f is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.66Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NADR_ECOLI This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the AMP moiety of ATP to nicotinamide ribonucleotide to form NAD(+). The NMN adenylyltransferase domain also functions as the NAD and ATP sensor.[1]

References

  1. Raffaelli N, Lorenzi T, Mariani PL, Emanuelli M, Amici A, Ruggieri S, Magni G. The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity. J Bacteriol. 1999 Sep;181(17):5509-11. PMID:10464228 doi:10.1128/JB.181.17.5509-5511.1999

8x7f, resolution 2.66Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA