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      Periplasmic form of dipeptidyl aminopeptidase IV from Pseudoxanthomonas mexicana WO24: purification, kinetic characterization, crystallization and X-ray crystallographic analysis

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          Abstract

          Dipeptidyl aminopeptidase IV (DAP IV or DPP IV) from Pseudoxanthomonas mexicana WO24 (PmDAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position [NH 2-P2-P1(Pro/Ala)-P1′-P2′…]. For crystallographic studies, the periplasmic form of PmDAP IV was overproduced in Escherichia coli, purified and crystallized in complex with the tripeptide Lys-Pro-Tyr using the hanging-drop vapour-diffusion method. Kinetic parameters of the purified enzyme against a synthetic substrate were also determined. X-ray diffraction data to 1.90 Å resolution were collected from a triclinic crystal form belonging to space group P1, with unit-cell parameters a = 88.66, b = 104.49, c = 112.84 Å, α = 67.42, β = 68.83, γ = 65.46°. Initial phases were determined by the molecular-replacement method using Stenotrophomonas maltophilia DPP IV (PDB entry 2ecf) as a template and refinement of the structure is in progress.

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          Author and article information

          Journal
          ACSFEN
          Acta Crystallographica Section F Structural Biology Communications
          Acta Crystallogr F Struct Biol Commun
          International Union of Crystallography (IUCr)
          2053-230X
          November 2017
          October 23 2017
          : 73
          : 11
          : 601-606
          Article
          10.1107/S2053230X17014911
          aeca3ea2-becd-4a18-85b1-32f1e60dc017
          © 2017

          http://journals.iucr.org/services/copyrightpolicy.html

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