7LIK
Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R
Summary for 7LIK
| Entry DOI | 10.2210/pdb7lik/pdb |
| EMDB information | 23379 23380 23381 23382 23383 23384 23385 |
| Descriptor | Maritimacin, RIBOFLAVIN (2 entities in total) |
| Functional Keywords | encapsulin, nanocompartment, virus like particle |
| Biological source | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
| Total number of polymer chains | 1 |
| Total formula weight | 30912.20 |
| 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 citation | Adamson, 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: 35119930DOI: 10.1126/sciadv.abl7346 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.91 Å) |
Structure validation
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