5iw4 | pdb_00005iw4

Crystal structure of E. coli NudC in complex with NAD

spinqualitylabelsall models 5iw4, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5iw4 is a 2 chain structure with sequence from Escherichia coli b354. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAD, ZN Related: 5iw5 Gene: nudC (Escherichia coli B354) Activity: NAD(+) diphosphatase, with EC number 3.6.1.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed RNA capping and decapping are thought to be distinctive features of eukaryotes. The redox cofactor NAD was recently discovered to be attached to small regulatory RNAs in bacteria in a cap-like manner, and Nudix hydrolase NudC was found to act as a NAD-decapping enzyme in vitro and in vivo. Here, crystal structures of Escherichia coli NudC in complex with substrate NAD and with cleavage product NMN reveal the catalytic residues lining the binding pocket and principles underlying molecular recognition of substrate and product. Biochemical mutation analysis identifies the conserved Nudix motif as the catalytic center of the enzyme, which needs to be homodimeric, as the catalytic pocket is composed of amino acids from both monomers. NudC is single-strand specific and has a purine preference for the 5'-terminal nucleotide. The enzyme strongly prefers NAD-linked RNA (NAD-RNA) over NAD and binds to a diverse set of cellular RNAs in an unspecific manner. Structure and function of the bacterial decapping enzyme NudC.,Hofer K, Li S, Abele F, Frindert J, Schlotthauer J, Grawenhoff J, Du J, Patel DJ, Jaschke A Nat Chem Biol. 2016 Sep;12(9):730-4. doi: 10.1038/nchembio.2132. Epub 2016 Jul, 18. PMID:27428510 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA