Cloning, purification and preliminary crystallographic analysis of the Helicobacter pylori leucyl aminopeptidase-bestatin complex

Joyanta K. Modak, Anna Roujeinikova

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Helicobacter pylori is an important human pathogenic bacterium associated with numerous severe gastroduodenal diseases, including ulcers and gastric cancer. Cytosolic leucyl aminopeptidase (LAP) is an important housekeeping protein that is involved in peptide and protein turnover, catabolism of proteins and modulation of gene expression. LAP is upregulated in metronidazole-resistant H. pylori, which suggests that, in addition to having an important housekeeping role, LAP contributes to the mechanism of drug resistance. Crystals of H. pylori LAP have been grown by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitating agent. The crystals belonged to the primitive triclinic space group P1, with unit-cell parameters a = 97.5, b = 100.2, c = 100.4 Å, [alpha] = 75.4, [beta] = 60.9, [gamma] = 81.8°. An X-ray diffraction data set was collected to 2.8 Å resolution from a single crystal. Molecular-replacement results using these data indicate that H. pylori LAP is a hexamer with 32 symmetry.
Original languageEnglish
Pages (from-to)1011-1014
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number9
Publication statusPublished - Sep 2013


  • heliobacter pylori
  • leucyl aminopeptidase
  • bestatin

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