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KMID : 0381920000300020185
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Korean Journal of Microscopy
2000 Volume.30 No. 2 p.185 ~ p.191
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Purification and Structural Characterization of P93 Complex from Hyperthermophilic Archaeon Thermococcus profundus
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Lee Mi-Hong
Kim Suk-Kyoung
Yun Young-Gun
Park Seong-Cheol
Park Jeong-Dong
Cheong Gang-Won
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Abstract
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An unusually large protein complex was found in the cytosol of the hyperthmophilic archaeon. Thermococcus profundus. The purified protein was shown to be a homomultimer of 93 kDa subunit (P93 complex). The complex is extremely heat stable. During 12 hrs incubation with SDS (final concentration 1%) at $85^{\circ}C$, no changed structure could be observed. Electron image analysis of negatively stained showed that the complex has a single, stable characteristic view and a well-preserved core with threefold rotational symmetry. The periphery of the assembly is composed of a nebulose, possibly flexible, component. Based on the projected structure suggest the P93 complex from T. profundus is composed 24 homomultimer.
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KEYWORD
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Electron Microscopy, Heat Stable, Hyperthermophilic Archaeon, Image Processing, Themococcus
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