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Solution structure of the cold-shock-like protein from Rickettsia rickettsii
Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since the R. rickettsii genome contains only one cold-shock-like protein and given the es...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3515365/ https://www.ncbi.nlm.nih.gov/pubmed/23143233 http://dx.doi.org/10.1107/S174430911203881X |
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author | Gerarden, Kyle P. Fuchs, Andrew M. Koch, Jonathan M. Mueller, Melissa M. Graupner, David R. O’Rorke, Justin T. Frost, Caleb D. Heinen, Heather A. Lackner, Emily R. Schoeller, Scott J. House, Paul G. Peterson, Francis C. Veldkamp, Christopher T. |
author_facet | Gerarden, Kyle P. Fuchs, Andrew M. Koch, Jonathan M. Mueller, Melissa M. Graupner, David R. O’Rorke, Justin T. Frost, Caleb D. Heinen, Heather A. Lackner, Emily R. Schoeller, Scott J. House, Paul G. Peterson, Francis C. Veldkamp, Christopher T. |
author_sort | Gerarden, Kyle P. |
collection | PubMed |
description | Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since the R. rickettsii genome contains only one cold-shock-like protein and given the essential nature of cold-shock proteins in other bacteria, the structure of the cold-shock-like protein from R. rickettsii was investigated. With the exception of a short α-helix found between β-strands 3 and 4, the solution structure of the R. rickettsii cold-shock-like protein has the typical Greek-key five-stranded β-barrel structure found in most cold-shock domains. Additionally, the R. rickettsii cold-shock-like protein, with a ΔG of unfolding of 18.4 kJ mol(−1), has a similar stability when compared with other bacterial cold-shock proteins. |
format | Online Article Text |
id | pubmed-3515365 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-35153652012-12-18 Solution structure of the cold-shock-like protein from Rickettsia rickettsii Gerarden, Kyle P. Fuchs, Andrew M. Koch, Jonathan M. Mueller, Melissa M. Graupner, David R. O’Rorke, Justin T. Frost, Caleb D. Heinen, Heather A. Lackner, Emily R. Schoeller, Scott J. House, Paul G. Peterson, Francis C. Veldkamp, Christopher T. Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since the R. rickettsii genome contains only one cold-shock-like protein and given the essential nature of cold-shock proteins in other bacteria, the structure of the cold-shock-like protein from R. rickettsii was investigated. With the exception of a short α-helix found between β-strands 3 and 4, the solution structure of the R. rickettsii cold-shock-like protein has the typical Greek-key five-stranded β-barrel structure found in most cold-shock domains. Additionally, the R. rickettsii cold-shock-like protein, with a ΔG of unfolding of 18.4 kJ mol(−1), has a similar stability when compared with other bacterial cold-shock proteins. International Union of Crystallography 2012-10-26 /pmc/articles/PMC3515365/ /pubmed/23143233 http://dx.doi.org/10.1107/S174430911203881X Text en © Gerarden et al. 2012 http://creativecommons.org/licenses/by/2.0/uk/ 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 authors and source are cited. |
spellingShingle | Structural Communications Gerarden, Kyle P. Fuchs, Andrew M. Koch, Jonathan M. Mueller, Melissa M. Graupner, David R. O’Rorke, Justin T. Frost, Caleb D. Heinen, Heather A. Lackner, Emily R. Schoeller, Scott J. House, Paul G. Peterson, Francis C. Veldkamp, Christopher T. Solution structure of the cold-shock-like protein from Rickettsia rickettsii |
title | Solution structure of the cold-shock-like protein from Rickettsia rickettsii
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title_full | Solution structure of the cold-shock-like protein from Rickettsia rickettsii
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title_fullStr | Solution structure of the cold-shock-like protein from Rickettsia rickettsii
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title_full_unstemmed | Solution structure of the cold-shock-like protein from Rickettsia rickettsii
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title_short | Solution structure of the cold-shock-like protein from Rickettsia rickettsii
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title_sort | solution structure of the cold-shock-like protein from rickettsia rickettsii |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3515365/ https://www.ncbi.nlm.nih.gov/pubmed/23143233 http://dx.doi.org/10.1107/S174430911203881X |
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