Sandbox Reserved 1052: Difference between revisions
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== Zinc Ligand(s) == | == Zinc Ligand(s) == | ||
</StructureSection> | </StructureSection> | ||
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paradigm ArsR family zinc sensor in the DNA-bound state. PNAS 106:43 | paradigm ArsR family zinc sensor in the DNA-bound state. PNAS 106:43 | ||
18177-18182 | 18177-18182 | ||
Penella M., Shokes J., Cosper N., Scott R.,Giedroc D. (2002). Structural elements | |||
of metal selectivity in metal sensor proteins. PNAS 100:7 3713-3718. | |||
Revision as of 13:49, 14 March 2017
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CzrA
Biological Function
Structural Overview
DNA Bound State
The main DNA interactions have been found to occur at the Ser 54 and 57 along with His 58. These residues are likely to interact with the 5'-TGAA sequence found in the half-site of the DNA. These residues are found in the N terminal of the R helix. The residues involved in the DNA binding pocket are Val 42 and Gln 53. This was experimentally determined by replacing the Gln and Val with Ala residues and measuring the binding capacity; the Ka decresed by 11 and 160-fold respectively[1] The previously mentioned Ser and His residues were found to bind the DNA with a similar affinity as the fully inhibited Zn2+.
Zinc Ligand(s)
</StructureSection>
References
Arunkumar A., Campanello G., Giedroc D. (2009). Solution Structure of a paradigm ArsR family zinc sensor in the DNA-bound state. PNAS 106:43 18177-18182
Penella M., Shokes J., Cosper N., Scott R.,Giedroc D. (2002). Structural elements of metal selectivity in metal sensor proteins. PNAS 100:7 3713-3718.
- ↑ [Arunkumar A., Campanello G., Giedroc D. (2009). Solution Structure of a paradigm ArsR family zinc sensor in the DNA-bound state. PNAS 106:43 18177-18182.]
