Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

Bacterial microcompartments (BMCs) consist of a protein shell and an encapsulated enzymatic core. Here, Kalnins et al. study a BMC from Klebsiella pneumoniae, show that the enzymatic core is encapsulated in a hierarchical manner, and solve the cryo-EM structure of a pT = 4 quasi-symmetric icosahedra...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Gints Kalnins, Eva-Emilija Cesle, Juris Jansons, Janis Liepins, Anatolij Filimonenko, Kaspars Tars
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3604a94c4ba740c0a775521e26530f60
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:3604a94c4ba740c0a775521e26530f60
record_format	dspace
spelling	oai:doaj.org-article:3604a94c4ba740c0a775521e26530f602021-12-02T17:31:24ZEncapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles10.1038/s41467-019-14205-y2041-1723https://doaj.org/article/3604a94c4ba740c0a775521e26530f602020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-14205-yhttps://doaj.org/toc/2041-1723Bacterial microcompartments (BMCs) consist of a protein shell and an encapsulated enzymatic core. Here, Kalnins et al. study a BMC from Klebsiella pneumoniae, show that the enzymatic core is encapsulated in a hierarchical manner, and solve the cryo-EM structure of a pT = 4 quasi-symmetric icosahedral shell particle.Gints KalninsEva-Emilija CesleJuris JansonsJanis LiepinsAnatolij FilimonenkoKaspars TarsNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Gints Kalnins Eva-Emilija Cesle Juris Jansons Janis Liepins Anatolij Filimonenko Kaspars Tars Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
description	Bacterial microcompartments (BMCs) consist of a protein shell and an encapsulated enzymatic core. Here, Kalnins et al. study a BMC from Klebsiella pneumoniae, show that the enzymatic core is encapsulated in a hierarchical manner, and solve the cryo-EM structure of a pT = 4 quasi-symmetric icosahedral shell particle.
format	article
author	Gints Kalnins Eva-Emilija Cesle Juris Jansons Janis Liepins Anatolij Filimonenko Kaspars Tars
author_facet	Gints Kalnins Eva-Emilija Cesle Juris Jansons Janis Liepins Anatolij Filimonenko Kaspars Tars
author_sort	Gints Kalnins
title	Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
title_short	Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
title_full	Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
title_fullStr	Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
title_full_unstemmed	Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
title_sort	encapsulation mechanisms and structural studies of grm2 bacterial microcompartment particles
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/3604a94c4ba740c0a775521e26530f60
work_keys_str_mv	AT gintskalnins encapsulationmechanismsandstructuralstudiesofgrm2bacterialmicrocompartmentparticles AT evaemilijacesle encapsulationmechanismsandstructuralstudiesofgrm2bacterialmicrocompartmentparticles AT jurisjansons encapsulationmechanismsandstructuralstudiesofgrm2bacterialmicrocompartmentparticles AT janisliepins encapsulationmechanismsandstructuralstudiesofgrm2bacterialmicrocompartmentparticles AT anatolijfilimonenko encapsulationmechanismsandstructuralstudiesofgrm2bacterialmicrocompartmentparticles AT kasparstars encapsulationmechanismsandstructuralstudiesofgrm2bacterialmicrocompartmentparticles
_version_	1718380604942188544

Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

Ejemplares similares