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7LIT

Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G

Summary for 7LIT
Entry DOI10.2210/pdb7lit/pdb
EMDB information23379 23380 23381 23382 23383 23384 23385
DescriptorMaritimacin, RIBOFLAVIN (2 entities in total)
Functional Keywordsencapsulin, nanocompartment, virus like particle
Biological sourceThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Total number of polymer chains1
Total formula weight29980.13
Authors
Andreas, M.P.,Adamson, L.,Tasneem, N.,Close, W.,Giessen, T.,Lau, Y.H. (deposition date: 2021-01-27, release date: 2022-02-09, Last modification date: 2024-05-29)
Primary citationAdamson, L.S.R.,Tasneem, N.,Andreas, M.P.,Close, W.,Jenner, E.N.,Szyszka, T.N.,Young, R.,Cheah, L.C.,Norman, A.,MacDermott-Opeskin, H.I.,O'Mara, M.L.,Sainsbury, F.,Giessen, T.W.,Lau, Y.H.
Pore structure controls stability and molecular flux in engineered protein cages.
Sci Adv, 8:eabl7346-eabl7346, 2022
Cited by
PubMed Abstract: 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.
PubMed: 35119930
DOI: 10.1126/sciadv.abl7346
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.53 Å)
Structure validation

227111

數據於2024-11-06公開中

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