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| Title | Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell. |
|---|---|
| Journal, issue, pages | Science, Vol. 356, Issue 6344, Page 1293-1297, Year 2017 |
| Publish date | Jun 23, 2017 |
 Authors | Markus Sutter / Basil Greber / Clement Aussignargues / Cheryl A Kerfeld /  |
| PubMed Abstract | Many bacteria contain primitive organelles composed entirely of protein. These bacterial microcompartments share a common architecture of an enzymatic core encapsulated in a selectively permeable ...Many bacteria contain primitive organelles composed entirely of protein. These bacterial microcompartments share a common architecture of an enzymatic core encapsulated in a selectively permeable protein shell; prominent examples include the carboxysome for CO fixation and catabolic microcompartments found in many pathogenic microbes. The shell sequesters enzymatic reactions from the cytosol, analogous to the lipid-based membrane of eukaryotic organelles. Despite available structural information for single building blocks, the principles of shell assembly have remained elusive. We present the crystal structure of an intact shell from , revealing the basic principles of bacterial microcompartment shell construction. Given the conservation among shell proteins of all bacterial microcompartments, these principles apply to functionally diverse organelles and can inform the design and engineering of shells with new functionalities. |
 External links | Science / PubMed:28642439 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 1.55 - 8.7 Å |
| Structure data |  EMDB-8747:  PDB-5v74:  PDB-5v75:  PDB-5v76: |
| Chemicals |  ChemComp-HOH:  ChemComp-GOL: |
| Source |
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 Keywords |  STRUCTURAL PROTEIN / BACTERIAL MICROCOMPARTMENTS |
