牙龈卟啉单胞菌二肽基肽酶11的结晶及初步X射线晶体学研究
Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis.
作者信息
Sakamoto Yasumitsu, Suzuki Yoshiyuki, Iizuka Ippei, Tateoka Chika, Roppongi Saori, Fujimoto Mayu, Gouda Hiroaki, Nonaka Takamasa, Ogasawara Wataru, Tanaka Nobutada
机构信息
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.
出版信息
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。
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