Transcriptional Regulation, Metal Binding Properties and Structure of Pden1597, an Unusual Zinc Transport Protein from Paracoccus denitrificans *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 290, Issue: 19, Page: 11878-11889
2015
- 19Citations
- 25Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations19
- Citation Indexes19
- 19
- CrossRef14
- Captures25
- Readers25
- 25
Article Description
ATP-binding cassette (ABC) transporters of the cluster 9 family are ubiquitous among bacteria and essential for acquiring Zn 2+ and Mn 2+ from the environment or, in the case of pathogens, from the host. These rely on a substrate-binding protein (SBP) to coordinate the relevant metal with high affinity and specificity and subsequently release it to a membrane permease for translocation into the cytoplasm. Although a number of cluster 9 SBP structures have been determined, the structural attributes conferring Zn 2+ or Mn 2+ specificity remain ambiguous. Here we describe the gene expression profile, in vitro metal binding properties, and crystal structure of a new cluster 9 SBP from Paracoccus denitrificans we have called AztC. Although all of our results strongly indicate Zn 2+ over Mn 2+ specificity, the Zn 2+ ion is coordinated by a conserved Asp residue only observed to date as a metal ligand in Mn 2+ -specific SBPs. The unusual sequence properties of this protein are shared among close homologues, including members from the human pathogens Klebsiella pneumonia and Enterobacter aerogenes, and would seem to suggest a subclass of Zn 2+ -specific transporters among the cluster 9 family. In any case, the unusual coordination environment of AztC expands the already considerable range of those available to Zn 2+ -specific SBPs and highlights the presence of a His-rich loop as the most reliable indicator of Zn 2+ specificity. Background: Bacterial cluster 9 ATP binding cassette (ABC) transporters are responsible for import of Zn 2+ and Mn 2+. Results: A solute-binding protein of the cluster 9 family is shown to preferentially bind Zn 2+ in an unusual coordination sphere. Conclusion: A subclass of Zn 2+ transporter has been identified with distinct structural properties. Significance: Cluster 9 ABC transporters are important virulence factors.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820485011; http://dx.doi.org/10.1074/jbc.m115.645853; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84929119863&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/25787075; https://linkinghub.elsevier.com/retrieve/pii/S0021925820485011; http://www.jbc.org/lookup/doi/10.1074/jbc.M115.645853; https://syndication.highwire.org/content/doi/10.1074/jbc.M115.645853; https://dx.doi.org/10.1074/jbc.m115.645853
Elsevier BV
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