3I96

Ethanolamine Utilization Microcompartment Shell Subunit, EutS

Summary for 3I96

• Entry DOI: 10.2210/pdb3i96/pdb
• Descriptor: Ethanolamine utilization protein eutS, CHLORIDE ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: structural protein
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 39273.60

Authors

Tanaka, S.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2009-07-10, release date: 2010-01-12, Last modification date: 2023-09-06)

Primary citation

Tanaka, S.,Sawaya, M.R.,Yeates, T.O.
Structure and Mechanisms of a Protein-Based Organelle in Escherichia coli.
Science, 327:81-84, 2010

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

Experimental method

X-RAY DIFFRACTION (1.65 Å)