Bacterial microcompartment organelles: protein shell structure and evolution. Yeates, T. O, Crowley, C. S, & Tanaka, S. Annual Review of Biophysics, February, 2010.
Bacterial microcompartment organelles: protein shell structure and evolution [link]Paper  doi  abstract   bibtex   
Some bacteria contain organelles or microcompartments consisting of a large virion-like protein shell encapsulating sequentially acting enzymes. These organized microcompartments serve to enhance or protect key metabolic pathways inside the cell. The variety of bacterial microcompartments provide diverse metabolic functions, ranging from CO(2) fixation to the degradation of small organic molecules. Yet they share an evolutionarily related shell, which is defined by a conserved protein domain that is widely distributed across the bacterial kingdom. Structural studies on a number of these bacterial microcompartment shell proteins are illuminating the architecture of the shell and highlighting its critical role in controlling molecular transport into and out of microcompartments. Current structural, evolutionary, and mechanistic ideas are discussed, along with genomic studies for exploring the function and diversity of this family of bacterial organelles. Expected final online publication date for the Annual Review of Biophysics Volume 39 is May 05, 2010. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.
@article{yeates_bacterial_2010,
	title = {Bacterial microcompartment organelles: protein shell structure and evolution},
	issn = {1936-1238},
	shorttitle = {Bacterial {Microcompartment} {Organelles}},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/20192762},
	doi = {10.1146/annurev.biophys.093008.131418},
	abstract = {Some bacteria contain organelles or microcompartments consisting of a large virion-like protein shell encapsulating sequentially acting enzymes. These organized microcompartments serve to enhance or protect key metabolic pathways inside the cell. The variety of bacterial microcompartments provide diverse metabolic functions, ranging from CO(2) fixation to the degradation of small organic molecules. Yet they share an evolutionarily related shell, which is defined by a conserved protein domain that is widely distributed across the bacterial kingdom. Structural studies on a number of these bacterial microcompartment shell proteins are illuminating the architecture of the shell and highlighting its critical role in controlling molecular transport into and out of microcompartments. Current structural, evolutionary, and mechanistic ideas are discussed, along with genomic studies for exploring the function and diversity of this family of bacterial organelles. Expected final online publication date for the Annual Review of Biophysics Volume 39 is May 05, 2010. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.},
	urldate = {2010-04-16TZ},
	journal = {Annual Review of Biophysics},
	author = {Yeates, Todd O and Crowley, Christopher S and Tanaka, Shiho},
	month = feb,
	year = {2010},
	pmid = {20192762}
}

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