3IO0
Crystal structure of EtuB from Clostridium kluyveri
Summary for 3IO0
| Entry DOI | 10.2210/pdb3io0/pdb |
| Descriptor | EtuB protein (2 entities in total) |
| Functional Keywords | tamdem repeat of bacterial microcompartment domain in a single polypeptide chain, structural protein |
| Biological source | Clostridium kluyveri DSM 555 |
| Total number of polymer chains | 1 |
| Total formula weight | 23756.20 |
| Authors | Pickersgill, R.W.,Warren, M.J. (deposition date: 2009-08-13, release date: 2009-09-15, Last modification date: 2024-02-21) |
| Primary citation | Heldt, D.,Frank, S.,Seyedarabi, A.,Ladakis, D.,Parsons, J.B.,Warren, M.J.,Pickersgill, R.W. Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilisation in Clostridium kluyveri. Biochem.J., 423:199-207, 2009 Cited by PubMed Abstract: 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. PubMed: 19635047DOI: 10.1042/BJ20090780 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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