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3D Representation of CzrA with Zn Bound

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CzrACzrA

Biological FunctionBiological Function

Structural OverviewStructural Overview

DNA Bound StateDNA Bound State

The 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 are Val 42 and Gln 53. This was experimentally determined by replacing the Gln and Val with Ala residues and measuring the binding capacity; In a previously published article[1], the DNA bound state of CzrA was tested by using the known critical residues for DNA interactions. Critical residues, Gln53, Val42, Ser54, Ser57, and His58, were replaced with Ala and then compared to the kinetics of the wild type protein. Replacing only the Q53 and V42 residues resulted in an 11-fold and 160-fold decrease in Ka, respectively. Other residues such as S54, S57, and H58 were also replaced with Ala residues, and it was found that these mutations caused binding similar to the fully inhibited Zn2+ bound state. Table 1 in this articel show the different Kobserved, and the measured decrease in Kobserved for each mutation.

Zinc Ligand(s)Zinc Ligand(s)

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ReferencesReferences

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.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Morgan Blake, Sarah Zimmerman, Geoffrey C. Hoops, Mary Liggett, Jakob Jozwiakowski