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3I82

Ethanolamine Utilization Microcompartment Shell Subunit, EutL Closed Form

Summary for 3I82
Entry DOI10.2210/pdb3i82/pdb
Related3I6P 3I71 3I87 3I96 3IA0
DescriptorEthanolamine utilization protein eutL (2 entities in total)
Functional Keywordsstructural protein
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight23875.93
Authors
Tanaka, S.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2009-07-09, release date: 2010-01-12, Last modification date: 2023-09-06)
Primary citationTanaka, S.,Sawaya, M.R.,Yeates, T.O.
Structure and Mechanisms of a Protein-Based Organelle in Escherichia coli.
Science, 327:81-84, 2010
Cited by
PubMed Abstract: Many bacterial cells contain proteinaceous microcompartments that act as simple organelles by sequestering specific metabolic processes involving volatile or toxic metabolites. Here we report the three-dimensional (3D) crystal structures, with resolutions between 1.65 and 2.5 angstroms, of the four homologous proteins (EutS, EutL, EutK, and EutM) that are thought to be the major shell constituents of a functionally complex ethanolamine utilization (Eut) microcompartment. The Eut microcompartment is used to sequester the metabolism of ethanolamine in bacteria such as Escherichia coli and Salmonella enterica. The four Eut shell proteins share an overall similar 3D fold, but they have distinguishing structural features that help explain the specific roles they play in the microcompartment. For example, EutL undergoes a conformational change that is probably involved in gating molecular transport through shell protein pores, whereas structural evidence suggests that EutK might bind a nucleic acid component. Together these structures give mechanistic insight into bacterial microcompartments.
PubMed: 20044574
DOI: 10.1126/science.1179513
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

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