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Crystallization and preliminary X-ray diffraction analysis of YejM from Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport
Salmonella typhimurium is responsible for over 35% of all foodborne illness related hospitalizations in the United States. This Gram-negative bacterium possesses an inner and an outer membrane (OM), the latter allowing its survival and replication within host tissues. During infection, OM is remode...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
F1000 Research Limited
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5728191/ https://www.ncbi.nlm.nih.gov/pubmed/29259761 http://dx.doi.org/10.12688/f1000research.8647.2 |
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author | Gabale, Uma Qian, Gene Roach, Elaina Ressl, Susanne |
author_facet | Gabale, Uma Qian, Gene Roach, Elaina Ressl, Susanne |
author_sort | Gabale, Uma |
collection | PubMed |
description | Salmonella typhimurium is responsible for over 35% of all foodborne illness related hospitalizations in the United States. This Gram-negative bacterium possesses an inner and an outer membrane (OM), the latter allowing its survival and replication within host tissues. During infection, OM is remodeled by transport of glycerophospholipids across the periplasm and into the OM. Increased levels of cardiolipin in the OM were observed upon PhoPQ activation and led to the discovery of YejM; an inner membrane protein essential for cell growth involved in cardiolipin binding and transport to the OM. Here we report how YejM was engineered to facilitate crystal growth and X-ray diffraction analysis. Successful structure determination of YejM will help us understand how they interact and how YejM facilitates cardiolipin transport to the OM. Ultimately, yejm, being an essential gene, may lead to new drug targets inhibiting the pathogenic properties of S. typhimurium. |
format | Online Article Text |
id | pubmed-5728191 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | F1000 Research Limited |
record_format | MEDLINE/PubMed |
spelling | pubmed-57281912017-12-18 Crystallization and preliminary X-ray diffraction analysis of YejM from Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport Gabale, Uma Qian, Gene Roach, Elaina Ressl, Susanne F1000Res Research Article Salmonella typhimurium is responsible for over 35% of all foodborne illness related hospitalizations in the United States. This Gram-negative bacterium possesses an inner and an outer membrane (OM), the latter allowing its survival and replication within host tissues. During infection, OM is remodeled by transport of glycerophospholipids across the periplasm and into the OM. Increased levels of cardiolipin in the OM were observed upon PhoPQ activation and led to the discovery of YejM; an inner membrane protein essential for cell growth involved in cardiolipin binding and transport to the OM. Here we report how YejM was engineered to facilitate crystal growth and X-ray diffraction analysis. Successful structure determination of YejM will help us understand how they interact and how YejM facilitates cardiolipin transport to the OM. Ultimately, yejm, being an essential gene, may lead to new drug targets inhibiting the pathogenic properties of S. typhimurium. F1000 Research Limited 2017-12-11 /pmc/articles/PMC5728191/ /pubmed/29259761 http://dx.doi.org/10.12688/f1000research.8647.2 Text en Copyright: © 2017 Gabale U et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Gabale, Uma Qian, Gene Roach, Elaina Ressl, Susanne Crystallization and preliminary X-ray diffraction analysis of YejM from Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
title | Crystallization and preliminary X-ray diffraction analysis of YejM from
Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
title_full | Crystallization and preliminary X-ray diffraction analysis of YejM from
Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
title_fullStr | Crystallization and preliminary X-ray diffraction analysis of YejM from
Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
title_full_unstemmed | Crystallization and preliminary X-ray diffraction analysis of YejM from
Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
title_short | Crystallization and preliminary X-ray diffraction analysis of YejM from
Salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
title_sort | crystallization and preliminary x-ray diffraction analysis of yejm from
salmonella typhimurium: an essential inner membrane protein involved in outer membrane directed cardiolipin transport |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5728191/ https://www.ncbi.nlm.nih.gov/pubmed/29259761 http://dx.doi.org/10.12688/f1000research.8647.2 |
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