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Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis.
Acta Crystallogr F Struct Biol Commun. 2015 Feb; 71(Pt 2):206-10.AC

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.

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Authors+Show Affiliations

Sakamoto Y
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Suzuki Y
Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Nigata 940-2188, Japan.
Iizuka I
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Tateoka C
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Roppongi S
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Fujimoto M
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Gouda H
School of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Nonaka T
School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Ogasawara W
Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Nigata 940-2188, Japan.
Tanaka N
School of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.

MeSH

Bacterial ProteinsCrystallizationCrystallography, X-RayDipeptidyl-Peptidases and Tripeptidyl-PeptidasesPorphyromonas gingivalis

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25664797

Citation

Sakamoto, Yasumitsu, et al. "Crystallization and Preliminary X-ray Crystallographic Studies of Dipeptidyl Peptidase 11 From Porphyromonas Gingivalis." Acta Crystallographica. Section F, Structural Biology Communications, vol. 71, no. Pt 2, 2015, pp. 206-10.
Sakamoto Y, Suzuki Y, Iizuka I, et al. Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis. Acta Crystallogr F Struct Biol Commun. 2015;71(Pt 2):206-10.
Sakamoto, Y., Suzuki, Y., Iizuka, I., Tateoka, C., Roppongi, S., Fujimoto, M., Gouda, H., Nonaka, T., Ogasawara, W., & Tanaka, N. (2015). Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis. Acta Crystallographica. Section F, Structural Biology Communications, 71(Pt 2), 206-10. https://doi.org/10.1107/S2053230X15000424
Sakamoto Y, et al. Crystallization and Preliminary X-ray Crystallographic Studies of Dipeptidyl Peptidase 11 From Porphyromonas Gingivalis. Acta Crystallogr F Struct Biol Commun. 2015;71(Pt 2):206-10. PubMed PMID: 25664797.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis. AU - Sakamoto,Yasumitsu, AU - Suzuki,Yoshiyuki, AU - Iizuka,Ippei, AU - Tateoka,Chika, AU - Roppongi,Saori, AU - Fujimoto,Mayu, AU - Gouda,Hiroaki, AU - Nonaka,Takamasa, AU - Ogasawara,Wataru, AU - Tanaka,Nobutada, Y1 - 2015/01/28/ PY - 2014/09/14/received PY - 2015/01/09/accepted PY - 2015/2/10/entrez PY - 2015/2/11/pubmed PY - 2015/11/3/medline KW - DPP11 KW - Porphyromonas gingivalis KW - dipeptidyl peptidase SP - 206 EP - 10 JF - Acta crystallographica. Section F, Structural biology communications JO - Acta Crystallogr F Struct Biol Commun VL - 71 IS - Pt 2 N2 - 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. SN - 2053-230X UR - https://www.unboundmedicine.com/medline/citation/25664797/Crystallization_and_preliminary_X_ray_crystallographic_studies_of_dipeptidyl_peptidase_11_from_Porphyromonas_gingivalis_ DB - PRIME DP - Unbound Medicine ER -