FEBS Letters | |
Crystallization of the bifunctional proteinase/amylase inhibitor PKI‐3 and of its complex with proteinase K | |
Betzel, Christian2  Pal, Gour P.2  Jany, Klaus-Dieter1  Saenger, Wolfram2  | |
[1] Institut für Organische Chemie, Biochemie und Isotopenforschung der Universität Stuttgart, Pfaffenwaldring 55, D-7000 Stuttgart 80, FRG;Institut für Kristallographie, Freie Universität Berlin, Takustr. 6, D-1000 Berlin 33, Germany | |
关键词: Bifunctional inhibitor Amylase Enzyme inhibitor Proteinase K X-ray diffraction Crystallization; | |
DOI : 10.1016/0014-5793(86)80308-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
One of the three wheat germ inhibitors of proteinase K is bifunctional and inhibits simultaneously proteinase K (or subtilisin but not enzymes of the trypsin family) and insect α-amylase. The molecular mass of this inhibitor called PKI-3 is 21 kDa, and the binding constant for proteinase K is 0.8 nM at pH 8.2, 25°C, in 1:1 molar ratio. PKI-3 was crystallized by microdialysis against 10–12% polyethylene glycol 6000, 50 mM NaH2PO4, pH 6.7. The crystals have monoclinic space group P21 with a = 42.5, b = 65.3, c = 31.5 Å, β = 110°, and diffract beyond 2.0 Å resolution. The complex proteinase K · PKI-3 was crystallized by equilibrium vapor diffusion under the same conditions. The crystals are needle-shaped and still too small for X-ray analysis. Gel electrophoresis established the composition of the crystals.
【 授权许可】
Unknown
【 预 览 】
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