Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri

Heldt, Dana, Frank, Stefanie, Seyedarabi, Arefeh, Ladikis, Dimitrios, Parsons, Joshua B., Warren, Martin J. ORCID: https://orcid.org/0000-0002-6028-6456 and Pickersgill, Richard W. (2009) Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri. Biochemical Journal, 423 (2). pp. 199-207. ISSN 0264-6021

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Abstract

It has been suggested that ethanol metabolism in the strict anaerobe Clostridium kluyveri occurs within a metabolosome, a subcellular proteinaceous bacterialmicrocompartment. 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.

Item Type: Article
Uncontrolled Keywords: bacterial microcompartment,clostridium kluyveri,ethanol utilization shell protein b (etub),metabolosome,organelle,pore,protein sheet,shell protein,biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School: Faculty of Science
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Depositing User: LivePure Connector
Date Deposited: 20 Sep 2022 15:31
Last Modified: 27 Sep 2022 08:37
URI: https://ueaeprints.uea.ac.uk/id/eprint/88526
DOI: 10.1042/BJ20090780

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