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- Title
Periplasmic form of dipeptidyl aminopeptidase IV from Pseudoxanthomonas mexicana WO24: purification, kinetic characterization, crystallization and X-ray crystallographic analysis.
- Authors
Roppongi, Saori; Tateoka, Chika; Fujimoto, Mayu; Iizuka, Ippei; Morisawa, Saori; Nakamura, Akihiro; Honma, Nobuyuki; Suzuki, Yoshiyuki; Shida, Yosuke; Ogasawara, Wataru; Tanaka, Nobutada; Sakamoto, Yasumitsu; Nonaka, Takamasa
- 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 [NH2-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 ) as a template and refinement of the structure is in progress.
- Subjects
AMINOPEPTIDASES; XANTHOMONAS; X-ray crystallography
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2017, Vol 73, Issue 11, p601
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X17014911