It has been suggested that ethanol metabolism in the strict anaerobe Clostridium kluyveri occurs within a metabolosome, a subcellular proteinaceous bacterial microcompartment. Two bacterial microcompartment shell proteins [EtuA (ethanol utilization shell protein A) and EtuB] are found encoded on the genome clustered with the genes for ethanol utilization. The function of the bacterial microcompartment is to facilitate fermentation by sequestering the enzymes, substrates and intermediates. Recent structural studies of bacterial microcompartment proteins have revealed both hexamers and pentamers that assemble to generate the pseudo-icosahedral bacterial microcompartment shell. Some of these shell proteins have pores on their symmetry axes. Here we report the structure of the trimeric bacterial microcompartment protein EtuB, which has a tandem structural repeat within the subunit and pseudo-hexagonal symmetry. The pores in the EtuB trimer are within the subunits rather than between symmetry related subunits. We suggest that the evolutionary advantage of this is that it releases the pore from the rotational symmetry constraint allowing more precise control of the fluxes of asymmetric molecules, such as ethanol, across the pore. We also model EtuA and demonstrate that the two proteins have the potential to interact to generate the casing for a metabolosome.
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Research Article|
September 25 2009
Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri
Dana Heldt;
Dana Heldt
*Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, U.K.
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Stefanie Frank;
Stefanie Frank
*Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, U.K.
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Arefeh Seyedarabi;
Arefeh Seyedarabi
†School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, U.K.
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Dimitrios Ladikis;
Dimitrios Ladikis
*Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, U.K.
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Joshua B. Parsons;
Joshua B. Parsons
*Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, U.K.
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Martin J. Warren;
Martin J. Warren
1
*Centre for Molecular Processing, School of Biosciences, University of Kent, Giles Lane, Canterbury, Kent CT2 7NJ, U.K.
1Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Richard W. Pickersgill
Richard W. Pickersgill
1
†School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, U.K.
1Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Publisher: Portland Press Ltd
Received:
May 21 2009
Revision Received:
July 28 2009
Accepted:
July 28 2009
Accepted Manuscript online:
July 28 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 423 (2): 199–207.
Article history
Received:
May 21 2009
Revision Received:
July 28 2009
Accepted:
July 28 2009
Accepted Manuscript online:
July 28 2009
Citation
Dana Heldt, Stefanie Frank, Arefeh Seyedarabi, Dimitrios Ladikis, Joshua B. Parsons, Martin J. Warren, Richard W. Pickersgill; Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri. Biochem J 15 October 2009; 423 (2): 199–207. doi: https://doi.org/10.1042/BJ20090780
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