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Insight into the Interaction of Metal Ions with TroA from Streptococcus suis

BACKGROUND: The scavenging ability of sufficient divalent metal ions is pivotal for pathogenic bacteria to survive in the host. ATP-binding cassette (ABC)-type metal transporters provide a considerable amount of different transition metals for bacterial growth. TroA is a substrate binding protein fo...

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Autores principales: Zheng, Beiwen, Zhang, Qiangmin, Gao, Jia, Han, Huiming, Li, Ming, Zhang, Jingren, Qi, Jianxun, Yan, Jinghua, Gao, George F.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3097204/
https://www.ncbi.nlm.nih.gov/pubmed/21611125
http://dx.doi.org/10.1371/journal.pone.0019510
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author Zheng, Beiwen
Zhang, Qiangmin
Gao, Jia
Han, Huiming
Li, Ming
Zhang, Jingren
Qi, Jianxun
Yan, Jinghua
Gao, George F.
author_facet Zheng, Beiwen
Zhang, Qiangmin
Gao, Jia
Han, Huiming
Li, Ming
Zhang, Jingren
Qi, Jianxun
Yan, Jinghua
Gao, George F.
author_sort Zheng, Beiwen
collection PubMed
description BACKGROUND: The scavenging ability of sufficient divalent metal ions is pivotal for pathogenic bacteria to survive in the host. ATP-binding cassette (ABC)-type metal transporters provide a considerable amount of different transition metals for bacterial growth. TroA is a substrate binding protein for uptake of multiple metal ions. However, the function and structure of the TroA homologue from the epidemic Streptococcus suis isolates (SsTroA) have not been characterized. METHODOLOGY/PRINCIPAL FINDINGS: Here we determined the crystal structure of SsTroA from a highly pathogenic streptococcal toxic shock syndrome (STSS)-causing Streptococcus suis in complex with zinc. Inductively coupled plasma mass spectrometry (ICP-MS) analysis revealed that apo-SsTroA binds Zn(2+) and Mn(2+). Both metals bind to SsTroA with nanomolar affinity and stabilize the protein against thermal unfolding. Zn(2+) and Mn(2+) induce distinct conformational changes in SsTroA compared with the apo form as confirmed by both circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra. NMR data also revealed that Zn(2+)/Mn(2+) bind to SsTroA in either the same site or an adjacent region. Finally, we found that the folding of the metal-bound protein is more compact than the corresponding apoprotein. CONCLUSIONS/SIGNIFICANCE: Our findings reveal a mechanism for uptake of metal ions in S. suis and this mechanism provides a reasonable explanation as to how SsTroA operates in metal transport.
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spelling pubmed-30972042011-05-24 Insight into the Interaction of Metal Ions with TroA from Streptococcus suis Zheng, Beiwen Zhang, Qiangmin Gao, Jia Han, Huiming Li, Ming Zhang, Jingren Qi, Jianxun Yan, Jinghua Gao, George F. PLoS One Research Article BACKGROUND: The scavenging ability of sufficient divalent metal ions is pivotal for pathogenic bacteria to survive in the host. ATP-binding cassette (ABC)-type metal transporters provide a considerable amount of different transition metals for bacterial growth. TroA is a substrate binding protein for uptake of multiple metal ions. However, the function and structure of the TroA homologue from the epidemic Streptococcus suis isolates (SsTroA) have not been characterized. METHODOLOGY/PRINCIPAL FINDINGS: Here we determined the crystal structure of SsTroA from a highly pathogenic streptococcal toxic shock syndrome (STSS)-causing Streptococcus suis in complex with zinc. Inductively coupled plasma mass spectrometry (ICP-MS) analysis revealed that apo-SsTroA binds Zn(2+) and Mn(2+). Both metals bind to SsTroA with nanomolar affinity and stabilize the protein against thermal unfolding. Zn(2+) and Mn(2+) induce distinct conformational changes in SsTroA compared with the apo form as confirmed by both circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra. NMR data also revealed that Zn(2+)/Mn(2+) bind to SsTroA in either the same site or an adjacent region. Finally, we found that the folding of the metal-bound protein is more compact than the corresponding apoprotein. CONCLUSIONS/SIGNIFICANCE: Our findings reveal a mechanism for uptake of metal ions in S. suis and this mechanism provides a reasonable explanation as to how SsTroA operates in metal transport. Public Library of Science 2011-05-18 /pmc/articles/PMC3097204/ /pubmed/21611125 http://dx.doi.org/10.1371/journal.pone.0019510 Text en Zheng et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Zheng, Beiwen
Zhang, Qiangmin
Gao, Jia
Han, Huiming
Li, Ming
Zhang, Jingren
Qi, Jianxun
Yan, Jinghua
Gao, George F.
Insight into the Interaction of Metal Ions with TroA from Streptococcus suis
title Insight into the Interaction of Metal Ions with TroA from Streptococcus suis
title_full Insight into the Interaction of Metal Ions with TroA from Streptococcus suis
title_fullStr Insight into the Interaction of Metal Ions with TroA from Streptococcus suis
title_full_unstemmed Insight into the Interaction of Metal Ions with TroA from Streptococcus suis
title_short Insight into the Interaction of Metal Ions with TroA from Streptococcus suis
title_sort insight into the interaction of metal ions with troa from streptococcus suis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3097204/
https://www.ncbi.nlm.nih.gov/pubmed/21611125
http://dx.doi.org/10.1371/journal.pone.0019510
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