<i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center

Bacterial type IV secretion systems (T4SSs) play central roles in antibiotic resistance spread and virulence. By cryo-electron tomography (CryoET), we solved the structure of the plasmid pKM101-encoded T4SS in the native context of the bacterial cell envelope.

Guardado en:
Detalles Bibliográficos
Autores principales: Pratick Khara, Liqiang Song, Peter J. Christie, Bo Hu
Formato: article
Lenguaje:EN
Publicado: American Society for Microbiology 2021
Materias:
Acceso en línea:https://doaj.org/article/5bdc36c14f5847b1a76295dde481f930
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:5bdc36c14f5847b1a76295dde481f930
record_format dspace
spelling oai:doaj.org-article:5bdc36c14f5847b1a76295dde481f9302021-11-03T21:52:35Z <i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center 2150-751110.1128/mBio.02465-21https://doaj.org/article/5bdc36c14f5847b1a76295dde481f9302021-10-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02465-21https://doaj.org/toc/2150-7511 Bacterial type IV secretion systems (T4SSs) play central roles in antibiotic resistance spread and virulence. By cryo-electron tomography (CryoET), we solved the structure of the plasmid pKM101-encoded T4SS in the native context of the bacterial cell envelope.Pratick KharaLiqiang SongPeter J. ChristieBo HuAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 12, Iss 5 (2021)
institution DOAJ
collection DOAJ
language EN
topic Microbiology
QR1-502
spellingShingle Microbiology
QR1-502
Pratick Khara
Liqiang Song
Peter J. Christie
Bo Hu
<i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center
description Bacterial type IV secretion systems (T4SSs) play central roles in antibiotic resistance spread and virulence. By cryo-electron tomography (CryoET), we solved the structure of the plasmid pKM101-encoded T4SS in the native context of the bacterial cell envelope.
format article
author Pratick Khara
Liqiang Song
Peter J. Christie
Bo Hu
author_facet Pratick Khara
Liqiang Song
Peter J. Christie
Bo Hu
author_sort Pratick Khara
title <i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center
title_short <i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center
title_full <i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center
title_fullStr <i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center
title_full_unstemmed <i>In Situ</i> Visualization of the pKM101-Encoded Type IV Secretion System Reveals a Highly Symmetric ATPase Energy Center
title_sort <i>in situ</i> visualization of the pkm101-encoded type iv secretion system reveals a highly symmetric atpase energy center
publisher American Society for Microbiology
publishDate 2021
url https://doaj.org/article/5bdc36c14f5847b1a76295dde481f930
work_keys_str_mv AT pratickkhara iinsituivisualizationofthepkm101encodedtypeivsecretionsystemrevealsahighlysymmetricatpaseenergycenter
AT liqiangsong iinsituivisualizationofthepkm101encodedtypeivsecretionsystemrevealsahighlysymmetricatpaseenergycenter
AT peterjchristie iinsituivisualizationofthepkm101encodedtypeivsecretionsystemrevealsahighlysymmetricatpaseenergycenter
AT bohu iinsituivisualizationofthepkm101encodedtypeivsecretionsystemrevealsahighlysymmetricatpaseenergycenter
_version_ 1718445396828618752