| Literature DB >> 25664797 |
Yasumitsu Sakamoto1, Yoshiyuki Suzuki2, Ippei Iizuka1, Chika Tateoka1, Saori Roppongi1, Mayu Fujimoto1, Hiroaki Gouda3, Takamasa Nonaka1, Wataru Ogasawara2, Nobutada Tanaka3.
Abstract
Dipeptidyl peptidase 11 from Porphyromonas gingivalis (PgDPP11) preferentially cleaves substrate peptides with Asp and Glu at the P1 position [NH2-P2-P1(Asp/Glu)-P1'-P2'...]. For crystallographic studies, PgDPP11 was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.82 Å resolution were collected from an orthorhombic crystal form belonging to space group C2221, with unit-cell parameters a = 99.33, b = 103.60, c = 177.33 Å. Structural analysis by the multi-wavelength anomalous diffraction method is in progress.Entities:
Keywords: DPP11; Porphyromonas gingivalis; dipeptidyl peptidase
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Year: 2015 PMID: 25664797 PMCID: PMC4321477 DOI: 10.1107/S2053230X15000424
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056