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TitleThe encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein.
Journal, issue, pagesSci Rep, Vol. 11, Issue 1, Page 22810, Year 2021
Publish dateNov 23, 2021
AuthorsBenjamin J LaFrance / Caleb Cassidy-Amstutz / Robert J Nichols / Luke M Oltrogge / Eva Nogales / David F Savage /
PubMed AbstractBacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based 'organelles' found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ...Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based 'organelles' found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~ 25-50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to create a unique chemical environment to facilitate catalysis and isolate toxic intermediates. Many questions regarding nanocompartment structure-function remain unanswered, including how shell symmetry dictates cargo loading and to what extent the shell facilitates enzymatic activity. Here, we explore these questions using the model Thermotoga maritima nanocompartment known to encapsulate a redox-active ferritin-like protein. Biochemical analysis revealed the encapsulin shell to possess a flavin binding site located at the interface between capsomere subunits, suggesting the shell may play a direct and active role in the function of the encapsulated cargo. Furthermore, we used cryo-EM to show that cargo proteins use a form of symmetry-matching to facilitate encapsulation and define stoichiometry. In the case of the Thermotoga maritima encapsulin, the decameric cargo protein with fivefold symmetry preferentially binds to the pentameric-axis of the icosahedral shell. Taken together, these observations suggest the shell is not simply a passive barrier-it also plays a significant role in the structure and function of the cargo enzyme.
External linksSci Rep / PubMed:34815415 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.0 Å
Structure data

24001

7mu1

EMDB-24001, PDB-7mu1:
Thermotoga maritima encapsulin shell
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-24002:
Cryo-EM map of the FLP cargo within the T. maritima encapsulin
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

Source
  • thermotoga maritima (bacteria)
KeywordsVIRUS LIKE PARTICLE / Encapsulin / Ferritin-like protein / EncFLP / Thermotoga / FMN / Bacterial Nanocompartment

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