Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments

Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):275-285. doi: 10.1107/S2053230X21007470. Epub 2021 Aug 24.

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.

Keywords: BMC; bacterial microcompartments; bacterial organelles; choline; glycyl radicals; shell proteins.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Choline / metabolism*
  • Crystallography, X-Ray
  • Escherichia coli / metabolism*
  • Organelles / metabolism*
  • Protein Conformation
  • Sequence Homology
  • Streptococcus intermedius / metabolism*

Substances

  • Bacterial Proteins
  • Choline