Structure and Mechanisms of a Protein-Based Organelle in Escherichia coli

Author:

Tanaka Shiho1,Sawaya Michael R.23,Yeates Todd O.134

Affiliation:

1. Department of Chemistry and Biochemistry, University of California Los Angeles, 611 Charles Young Drive East, Los Angeles, CA 90095, USA.

2. Howard Hughes Medical Institute, University of California Los Angeles, 611 Charles Young Drive East, Los Angeles, CA 90095, USA.

3. Univeristy of California Los Angeles, Department of Energy Institute for Genomics and Proteomics, 611 Charles Young Drive East, Los Angeles, CA 90095, USA.

4. Molecular Biology Institute, University of California Los Angeles 611 Charles Young Drive East, Los Angeles, CA 90095, USA.

Abstract

Bacterial Compartmentalization In diverse bacteria, reactions that involve toxic or volatile metabolites are carried out by enzymes inside proteinaceous microcompartments. Tanaka et al. (p. 81 ; see the Perspective by Kang and Douglas ) now report high-resolution crystal structures for four homologous proteins that are constituents of the shell that sequesters the metabolism of ethanolamine in bacteria. While the structures have similar overall folds, they have distinctive structural features that provide insight into how they build the shell and participate in microcompartment function.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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