Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis

被引：1

作者：

Sakamoto, Yasumitsu ^{[1
]}

Suzuki, Yoshiyuki ^{[2
]}

Iizuka, Ippei ^{[1
]}

Tateoka, Chika ^{[1
]}

Roppongi, Saori ^{[1
]}

Fujimoto, Mayu ^{[1
]}

Gouda, Hiroaki ^{[3
]}

Nonaka, Takamasa ^{[1
]}

Ogasawara, Wataru ^{[2
]}

Tanaka, Nobutada ^{[3
]}

机构：

[1] Iwate Med Univ, Sch Pharm, Yahaba, Iwate 0283694, Japan

[2] Nagaoka Univ Technol, Dept Bioengn, Nagaoka, Niigata 9402188, Japan

[3] Showa Univ, Sch Pharm, Shinagawa Ku, Tokyo 1428555, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷

关键词：

dipeptidyl peptidase; DPP11; Porphyromonas gingivalis; CRYSTAL-STRUCTURE; EXOPEPTIDASES; DISEASE;

D O I：

10.1107/S2053230X15000424

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom resolution were collected from an orthorhombic crystal form belonging to space group C222(1), with unit-cell parameters a = 99.33, b = 103.60, c = 177.33 angstrom. Structural analysis by the multi-wavelength anomalous diffraction method is in progress.

引用

页码：206 / 210

页数：5

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