Sandbox20: Difference between revisions
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Before the structure of the Tus-Ter complex was determined, mutation of Glu49 was shown to eliminate anti-helicase activity without affecting DNA binding. This could not be explained by the [[1ecr|original crystal structure]] as it is not located close enough to make direct contact with the conserved cytosine. However, the [[2ewj|more recent structure]] revealed that this is due the water-mediated hydrogen bond formed between it and the adenine residue adjacent to cytosine. It is therefore likely, that the interaction is necessary to compensate for the disrupted H-bonding in the nucleotide adjacent to the displaced cytosine, as shown in this <scene name='Sandbox20/Tus/18'>model</scene>. | Before the structure of the Tus-Ter complex was determined, mutation of Glu49 was shown to eliminate anti-helicase activity without affecting DNA binding. This could not be explained by the [[1ecr|original crystal structure]] as it is not located close enough to make direct contact with the conserved cytosine. However, the [[2ewj|more recent structure]] revealed that this is due the water-mediated hydrogen bond formed between it and the adenine residue adjacent to cytosine. It is therefore likely, that the interaction is necessary to compensate for the disrupted H-bonding in the nucleotide adjacent to the displaced cytosine, as shown in this <scene name='Sandbox20/Tus/18'>model</scene>. | ||
Index of Tus scenes: [1] <scene name='Sandbox20/Tus/2'>Original</scene>, [2] <scene name='Sandbox20/Tus/19'>DNA binding</scene>, [3] <scene name='Sandbox20/Tus/13'>Conserved cytosine</scene>, [4] <scene name='Sandbox20/Tus/9'>Cytosine displacement</scene>, [5] <scene name='Sandbox20/Tus/18'>E49 hydrogen bond</scene>. |