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Structure paper

TitlePore structure controls stability and molecular flux in engineered protein cages.
Journal, issue, pagesSci Adv, Vol. 8, Issue 5, Page eabl7346, Year 2022
Publish dateFeb 4, 2022
AuthorsLachlan S R Adamson / Nuren Tasneem / Michael P Andreas / William Close / Eric N Jenner / Taylor N Szyszka / Reginald Young / Li Chen Cheah / Alexander Norman / Hugo I MacDermott-Opeskin / Megan L O'Mara / Frank Sainsbury / Tobias W Giessen / Yu Heng Lau /
PubMed AbstractProtein cages are a common architectural motif used by living organisms to compartmentalize and control biochemical reactions. While engineered protein cages have featured in the construction of ...Protein cages are a common architectural motif used by living organisms to compartmentalize and control biochemical reactions. While engineered protein cages have featured in the construction of nanoreactors and synthetic organelles, relatively little is known about the underlying molecular parameters that govern stability and flux through their pores. In this work, we systematically designed 24 variants of the encapsulin cage, featuring pores of different sizes and charges. Twelve pore variants were successfully assembled and purified, including eight designs with exceptional thermal stability. While negatively charged mutations were better tolerated, we were able to form stable assemblies covering a full range of pore sizes and charges, as observed in seven new cryo-EM structures at 2.5- to 3.6-Å resolution. Molecular dynamics simulations and stopped-flow experiments revealed the importance of considering both pore size and charge, together with flexibility and rate-determining steps, when designing protein cages for controlling molecular flux.
External linksSci Adv / PubMed:35119930 / PubMed Central
MethodsEM (single particle)
Resolution2.53 - 3.55 Å
Structure data

23379

7lii

EMDB-23379, PDB-7lii:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D
Method: EM (single particle) / Resolution: 3.55 Å

23380

7lij

EMDB-23380, PDB-7lij:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K
Method: EM (single particle) / Resolution: 2.84 Å

23381

7lik

EMDB-23381, PDB-7lik:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R
Method: EM (single particle) / Resolution: 2.91 Å

23382

7lil

EMDB-23382, PDB-7lil:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3
Method: EM (single particle) / Resolution: 2.84 Å

23383

7lim

EMDB-23383, PDB-7lim:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E
Method: EM (single particle) / Resolution: 2.75 Å

23384

7lis

EMDB-23384, PDB-7lis:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D
Method: EM (single particle) / Resolution: 2.96 Å

23385

7lit

EMDB-23385, PDB-7lit:
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G
Method: EM (single particle) / Resolution: 2.53 Å

Chemicals

ChemComp-RBF:
RIBOFLAVIN

Source
  • Thermotoga maritima MSB8 (bacteria)
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
KeywordsVIRUS LIKE PARTICLE / Encapsulin / Nanocompartment

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