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羧酶体--carboxysomes

已有 8940 次阅读 2008-10-28 20:23 |个人分类:微生物生理学专栏|关键词:羧酶体--carboxysomes| 羧酶体--carboxysomes

 

 

Figure(Up). Cartoon representation of the carboxysome, indicating some of the protein components involved, and showing the recently determined structures of the major shell proteins

The CcmK/Csos1 proteins (lower right) form hexamers that pack into a two-dimensional molecular layer. Narrow electrostatically positive pores through the layer may serve to transport negatively charged small molecules (such as bicarbonate) into and out of the carboxysome.

 

Figure up. UCLA chemists are studying the structure of a protein shell called the carboxysome. The pentagons (shown in red) sit at the corners of the shell and are critical for causing an otherwise flat layer of hexagons to close.
Credit: Todd O. Yeates/UCLA Chemistry and Biochemistry

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The carboxysome is the best characterized example of a bacterial microcompartment. Bacterial microcompartments are simple organelles that act to sequester specific metabolic pathways inside many bacteria. The carboxysome encapsulates the enzymes required for CO2 fixation, namely RuBisCO and carbonic anhydrase, inside a proteinaceaous shell resembling a large viral capsid roughly 1200 Angstroms in diameter. Carboxysomes are present in all cyanobacteria and many chemoautotrophs, where they dramatically enhance the efficiency of carbon fixation by providing a concentrated source of CO2 for RuBisCO, whose relatively low reactivity and selectivity towards CO2 is problematic. Carboxysomes were first identified and characterized more than 30 years ago, but their structures have only recently come under systematic investigation. Cheryl Kerfeld, Shiho Tanaka, and Yingssu Tsai have determined the crystal structures of several proteins that make up the shell of the carboxysome. The hexameric units pack to form tight layers of molecules with small pores through which only small metabolites (e.g. bicarbonate, 3PGA, and 5RuBP) can pass. Pentameric proteins appear to form the vertices of the icosahedral shell. Three-dimensional structures of the component proteins make it possible now to ask specific questions about architecture, biochemical mechanisms, and evolutionary relationships. A number of intriguing questions remain, not the least of which is how the shell manages to recognize and encapsulate all the RuBisCO in the cell. Investigations of related but functionally distinct microcompartments, including those in E. coli and Salmonella, are just beginning.

References:

强烈推荐2008年九月份Nature上的一篇综述:

Protein-based organelles in bacteria: carboxysomes and related microcompartments (downlond).

Shiho Tanaka, Cheryl A. Kerfeld, Michael R. Sawaya, Fei Cai, Sabine Heinhorst, Gordon C. Cannon and Todd O. YeatesAtomic-Level Models of the Bacterial Carboxysome Shell.Science 22 February 2008: Vol. 319. no. 5866, pp. 1083 - 1086.  (downlond-0)

Kerfeld, C.A., Sawaya, M.R., Tanaka, S., Nguyen, C.V., Phillips, M., Beeby, M., Yeates, T.O. 2005. Protein structures forming the shell of primitive bacterial organelles.? Science 309, 936-8. (downlond-2)

Tsai, Y., Sawaya, M.R., Cannon, G.C., Cai, F., Williams, E.B., Heinhorst, S., Kerfeld, C.A., and Yeates, T.O. (2007). Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome. PLoS Biol. ?5, e144.(downlond-3)

Yeates, T.O., Tsai, Y., Tanaka, S., Sawaya, M.R., Kerfeld, C.A. (2007). Self-assembly in the carboxysome: a viral capsid-like protein shell in bacterial cells. Biochem. Soc. Trans. 35, 508-11. download-1

 

 



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