Sandbox Reserved 1052: Difference between revisions
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Mary Liggett (talk | contribs) No edit summary |
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<Structure load='2KJB' size='350' frame='true' align='left' caption='3D Representation of CzrA with Zn Bound' scene='Insert optional scene name here' /> | <Structure load='2KJB' size='350' frame='true' align='left' caption='3D Representation of CzrA with Zn Bound' scene='Insert optional scene name here' /> | ||
==CzrA== | ==CzrA== | ||
== Biological Function == | == Biological Function == | ||
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== DNA Bound State == | == DNA Bound State == | ||
The <scene name='69/694219/Serandhisresidues/2'>main DNA interactions</scene> have been found to occur at the | 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 | ||
paradigm ArsR family zinc sensor in the DNA-bound state. PNAS 106:43 | |||
18177-18182.]</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>. | |||
== Zinc Ligand(s) == | == Zinc Ligand(s) == | ||
== Other Ligands == | == Other Ligands == | ||
</StructureSection> | </StructureSection> | ||
== References == | == 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 |