Celina Pinto/Sandbox 211: Difference between revisions

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T5 5'-exonuclease is a homodimeric protein composed of two identical chains, <scene name='Celina_Pinto/Sandbox_211/Chain_a/2'>chain a</scene> and <scene name='Celina_Pinto/Sandbox_211/Chain_b/1'>chain b</scene>. Both chains contain a hole, bound by a <scene name='Celina_Pinto/Sandbox_211/Helical_arch/2'>helical arch</scene> composed of two helices in which  
T5 5'-exonuclease is a homodimeric protein composed of two identical chains, <scene name='Celina_Pinto/Sandbox_211/Chain_a/3'>TextToBeDisplayed</scene> and <scene name='Celina_Pinto/Sandbox_211/Chain_b/2'>chain b</scene>. Both chains contain a hole, bound by a <scene name='Celina_Pinto/Sandbox_211/Helical_arch/2'>helical arch</scene> composed of two helices in which  
<scene name='Celina_Pinto/Sandbox_211/Residues_helical_arch/2'>hydrophobic and positively charged residues</scene> are located. The helical arch is situated in front of the active site and only single-stranded DNA can pass through it. Since the enzyme is able to cleave double-stranded DNA, the enzyme has a conformational flexibility to facilitate DNA threading which is required to process the 5' nuclease substrates in the active site.  
<scene name='Celina_Pinto/Sandbox_211/Residues_helical_arch/2'>hydrophobic and positively charged residues</scene> are located. The helical arch is situated in front of the active site and only single-stranded DNA can pass through it. Since the enzyme is able to cleave double-stranded DNA, the enzyme has a conformational flexibility to facilitate DNA threading which is required to process the 5' nuclease substrates in the active site.  


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Celina Pinto