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Updated: Oct 21, 2025

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial
Jessica M Ochoa1, Oscar Mijares2, Andrea A Acosta2
1UCLA Molecular Biology Institute, University of California Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095, USA.
Abstract:
Bacterial microcompartments are large supramolecular structures comprising an outer proteinaceous shell that encapsulates various enzymes in order to optimize metabolic processes. The outer shells of bacterial microcompartments are made of several thousand protein subunits, generally forming hexameric building blocks based on the canonical bacterial microcompartment (BMC) domain. Among the diverse metabolic types of bacterial microcompartments, the structures of those that use glycyl radical enzymes to metabolize choline have not been adequately characterized. Here, six structures of hexameric shell proteins from type I and type II choline-utilization microcompartments are reported. Sequence and structure analysis reveals electrostatic surface properties that are shared between the four types of shell proteins described here.
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