6ehi | pdb_00006ehi

NucT from Helicobacter pylori

spinqualitylabelsall models 6ehi, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ehi is a 12 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: ACT, CL, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1V3AA65_HELPX Publication Abstract from PubMed The Phospholipase D (PLD) superfamily of proteins includes a group of enzymes with nuclease activity on various nucleic acid substrates. Here, with the aim of better understanding the substrate specificity determinants in this subfamily, we have characterised the enzymatic activity and the crystal structure of NucT, a nuclease implicated in Helicobacter pylori purine salvage and natural transformation and compared them to those of its bacterial and mammalian homologues. NucT exhibits an endonuclease activity with a strong preference for single stranded nucleic acids substrates. We identified histidine124 as essential for the catalytic activity of the protein. Comparison of the NucT crystal structure at 1.58 A resolution reported here with those of other members of the sub-family suggests that the specificity of NucT for single-stranded nucleic acids is provided by the width of a positively charged groove giving access to the catalytic site. Structural basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity.,Celma L, Corbinais C, Vercruyssen J, Veaute X, de la Sierra-Gallay IL, Guerois R, Busso D, Mathieu A, Marsin S, Quevillon-Cheruel S, Radicella JP PLoS One. 2017 Dec 4;12(12):e0189049. doi: 10.1371/journal.pone.0189049., eCollection 2017. PMID:29206236 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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