Sakamoto Yasumitsu, Suzuki Yoshiyuki, Iizuka Ippei, Tateoka Chika, Roppongi Saori, Fujimoto Mayu, Gouda Hiroaki, Nonaka Takamasa, Ogasawara Wataru, Tanaka Nobutada
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Nigata 940-2188, Japan.
Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):206-10. doi: 10.1107/S2053230X15000424. Epub 2015 Jan 28.
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.
牙龈卟啉单胞菌的二肽基肽酶11（PgDPP11）优先切割在P1位置带有天冬氨酸（Asp）和谷氨酸（Glu）的底物肽[NH2-P2-P1（Asp/Glu）-P1'-P2'...]。为了进行晶体学研究，PgDPP11在大肠杆菌中过量表达，通过悬滴气相扩散法进行纯化和结晶。从属于空间群C2221的正交晶型收集了分辨率为1.82 Å的X射线衍射数据，晶胞参数为a = 99.33、b = 103.60、c = 177.33 Å。目前正在通过多波长反常衍射法进行结构分析。
