Sand box 211: Difference between revisions

Michal Harel (talk | contribs)
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Michal Harel (talk | contribs)
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== '''Structure''' ==
== '''Structure''' ==


<Structure load='1EXN' size='350' frame='true' align='right' caption='T5 phage exonuclease' scene='Insert optional scene name here' />
<Structure load='1EXN' size='350' frame='true' align='right' caption='T5 phage exonuclease (PDB code [[1exn]])' scene='Insert optional scene name here' />
<scene name='Sand_box_211/1exn/4'>T5 5'-exonuclease</scene> is a homodimeric protein composed of two identical chains,<scene name='Sand_box_211/Vghjvjh/4'>chain a</scene> and <scene name='Sand_box_211/Vhj/3'>chain b</scene>.
<scene name='Sand_box_211/1exn/4'>T5 5'-exonuclease</scene> is a homodimeric protein composed of two identical chains,<scene name='Sand_box_211/Vghjvjh/4'>chain a</scene> and <scene name='Sand_box_211/Vhj/3'>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<ref>PMID:8657312</ref>. 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.  
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<ref>PMID:8657312</ref>. 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, Michal Harel