8igi

Crystal structure of HP1526 (XthA)- a base excision DNA repair protein in Helicobacter pylori

spinqualitylabelsall models 8igi, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8igi is a 2 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Ligands: BU2, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O26054_HELPY Publication Abstract from PubMed Helicobacter pylori is a bacterium that causes gastritis, peptic ulcer disease and adenocarcinoma while infecting human stomach. In the stomach H. pylori is under stresses caused by reactive oxygen and nitrogen species from host immune response, which causes oxidative DNA damage. The DNA damage in single base is repaired by base excision repair (BER) and/or nucleotide incision repair (NIR) pathways. H. pylori retains a minimal set of enzymes involved in the BER and NIR pathways. The HP1526 protein is a single apurinic/apyrimidinic (AP) endonuclease homologous to E. coli Xth protein but little is known for its structure up to now. In this study, the structure of the recombinant HP1526 protein from H. pylori (HpXthA) has been determined at a high resolution of 1.84 A. From the structural analysis the HpXthA was found to belong to the Xth-like AP endonuclease family carrying the common fold of a central bilayer beta-sheet flanked by alpha-helices with a divalent metal ion bound. A Mn(2+) ion and a 1,3-butanediol were unusually found and modeled around the active site. Structural and sequence comparisons among the AP endonucleases show well-conserved residues for metal and DNA binding and for catalysis. Interestingly, the presence of a small polar residue Ser201 of the HpXthA commonly found in NIR-proficient AP endonucleases instead of an aspartate residue in NIR-deficient enzymes suggests that the HpXthA retain a nucleotide incision repair activity. Crystal structure of the apurinic/apyrimidinic endonuclease XthA (HP1526 protein) from Helicobacter pylori.,Dinh T, Dao O, Killivalavan A, Ngo D, Lee KH Biochem Biophys Res Commun. 2023 Jun 30;663:8-15. doi: , 10.1016/j.bbrc.2023.04.047. Epub 2023 Apr 19. PMID:37116395 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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