Sandbox Reserved 1052: Difference between revisions

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

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 == DNA Bound State ==
-The <scene name='69/694219/Serandhisresidues/2'>main DNA interactions</scene> 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 <scene name='69/694219/Dna_binding_pocket/1'>DNA binding pocket</scene> 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<ref name="LoC">[Arunkumar A., Campanello G., Giedroc D. (2009). Solution Structure of a
+The <scene name='69/694219/Serandhisresidues/2'>main DNA interactions</scene> 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 <scene name='69/694219/Dna_binding_pocket/1'>DNA binding pocket</scene> 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<ref name="LoC">[Arunkumar A., Campanello G., Giedroc D. (2009). Solution Structure of a
 paradigm ArsR family zinc sensor in the DNA-bound state. PNAS 106:43
--18182.]</ref> The previously mentioned Ser and His residues were found to bind the DNA with a similar affinity as the fully inhibited Zn<sup>2+</sup>.
+-18182.]</ref>, 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 K<sub>a</sub>, 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 Zn<sup>2+</sup> bound state. Table 1 in this articel show the different K<sub>observed</sub>, and the measured decrease in K<sub>observed</sub> for each mutation.
 == Zinc Ligand(s) ==