The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Metalloregulatory proteins: Metal selectivity and allosteric switching
Open accessAbstract
Prokaryotic organisms have evolved an impressive capacity to quickly adapt to a changing and challenging microenvironment in which the availability of both biologically required and non-essential transition metal ions can vary dramatically. In all bacteria, a panel of metalloregulatory proteins control the expression of genes encoding membrane transporters and metal trafficking proteins, that collectively manage metal homeostasis and resistance. These “metal sensors” are specialized allosteric proteins, in which the direct binding of a specific or small number of “cognate” metal ion(s) drives a conformational change in the regulator that allosterically activates or inhibits operator DNA binding, or alternatively, distorts the promoter structure thereby converting a poor promoter to a strong one. In this review, we discuss our current understanding of the features that control metal specificity of the allosteric response in these systems, and the role that structure, thermodynamics and conformational dynamics play in mediating allosteric activation or inhibition of DNA binding.
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Citations
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Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation
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Metadata
- Authors
- Reyes-Caballero, H., Campanello, G. C., & Giedroc, D. P.
- Venue
- Biophysical Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 156
- Issue
- 2-3
- Pages
- 103-114
- ISSN
- 0301-4622 (ISSN-L)
- OpenAlex
- W2037763527
- Cited by
- 172
- References
- 19
- FWCI
- 9.68
- Type
- journal article
- Language
- en
- Open access
- green
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