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1.
Acta Crystallogr F Struct Biol Commun ; 73(Pt 11): 601-606, 2017 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-29095153

RESUMO

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 Šresolution 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, ß = 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.


Assuntos
Dipeptidil Peptidase 4/química , Dipeptidil Peptidase 4/isolamento & purificação , Periplasma/enzimologia , Xanthomonadaceae/enzimologia , Cristalização , Cristalografia por Raios X , Dipeptidil Peptidase 4/metabolismo , Cinética , Conformação Proteica , Xanthomonadaceae/classificação
2.
Acta Crystallogr F Struct Biol Commun ; 70(Pt 2): 221-4, 2014 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24637761

RESUMO

Dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24 (DAP BII) is able to cleave a variety of dipeptides from the amino-terminus of substrate peptides. For crystallographic studies, DAP BII was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 2.3 Å resolution were collected using an orthorhombic crystal form belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.55, b = 130.86, c = 170.87 Å. Structural analysis by the multi-wavelength anomalous diffraction method is in progress.


Assuntos
Cristalografia por Raios X/métodos , Dipeptidil Peptidases e Tripeptidil Peptidases/química , Xanthomonadaceae/enzimologia , Cristalização , Conformação Proteica , Proteínas Recombinantes/química
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