Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments
| Autor: | Michael R. Sawaya, Nancy Leon-Rivera, Andrea A Acosta, Xavier Escoto, Jessica M Ochoa, Todd O. Yeates, Oscar Mijares, Joanna D Marshall |
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| Rok vydání: | 2021 |
| Předmět: |
Structure analysis
Protein Conformation Protein subunit Biophysics Shell (structure) Supramolecular chemistry Sequence Homology Sequence (biology) Crystallography X-Ray Biochemistry Research Communications Choline chemistry.chemical_compound Bacterial Proteins Structural Biology Bacterial microcompartment Escherichia coli Genetics Amino Acid Sequence Organelles chemistry.chemical_classification Condensed Matter Physics Enzyme chemistry Streptococcus intermedius |
| Zdroj: | Acta Crystallogr F Struct Biol Commun |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x21007470 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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