<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.
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American Society for Microbiology
2021
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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) |
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Microbiology QR1-502 |
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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 |