Sandbox 666: Difference between revisions

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''Eco''RI is composed of two homodimers, so it has two identical subunits (Representation of one <scene name='Sandbox_666/Monomer_structure/4'>subunit</scene>) of 31 kDa, but it is possible to have homotetramers at high concentrations. The constitutive monomers are 276 amino acids long. ''Eco''RI and all the other restriction enzymes show a common structural core, which is a α/β domain. The constitutive subunits of ''Eco''RI are organized into a single α/β domain (five strands <scene name='Sandbox_666/B_sheet/1'>β</scene> sheet, which is surrounded by <scene name='Sandbox_666/Helix/1'>two α helices</scene> ). Four of these five β strands are parallel whereas the fourth (β4) is in an anti-parallel orientation to the others.<ref name="B">Refinement of ''Eco''RI endonuclease crystal structure: a revised protein chain tracing.

''Eco''RI is composed of two homodimers, so it has two identical subunits (Representation of one <scene name='Sandbox_666/Monomer_structure/4'>subunit</scene>) of 31 kDa, but it is possible to have homotetramers at high concentrations. The constitutive monomers are 276 amino acids long. ''Eco''RI and all the other restriction enzymes show a common structural core, which is a α/β domain. The constitutive subunits of ''Eco''RI are organized into a single α/β domain (five strands <scene name='Sandbox_666/B_sheet/1'>β</scene> sheet, which is surrounded by <scene name='Sandbox_666/Helix/1'>two α helices</scene> ). Four of these five β strands are parallel whereas the fourth (β4) is in an anti-parallel orientation to the others.<ref name="B">Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracing.

Kim YC, Grable JC, Love R, Greene PJ, Rosenberg JM.</ref>

Kim, Y.C., Grable, J.C., Love, R., Greene, P.J., Rosenberg, J.M.,

Journal: (1990) Science 249: 1307-1309 </ref>

[[Image:Image1 EcoRI.png |thumb| The topology of EcoRI restriction endonuclease |left| 400px]]

Sandbox 666: Difference between revisions

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 {{STRUCTURE_1eri| PDB=1eri | SCENE= | size='500'}}
-''Eco''RI is composed of two homodimers, so it has two identical subunits (Representation of one <scene name='Sandbox_666/Monomer_structure/4'>subunit</scene>) of 31 kDa, but it is possible to have homotetramers at high concentrations. The constitutive monomers are 276 amino acids long. ''Eco''RI and all the other restriction enzymes show a common structural core, which is a  α/β domain. The constitutive subunits of ''Eco''RI are organized into a single α/β domain (five strands <scene name='Sandbox_666/B_sheet/1'>β</scene> sheet, which is surrounded  by <scene name='Sandbox_666/Helix/1'>two α helices</scene> ). Four of these five β strands are parallel whereas the fourth (β4) is in an anti-parallel orientation to the others.<ref name="B">Refinement of ''Eco''RI endonuclease crystal structure: a revised protein chain tracing.
+''Eco''RI is composed of two homodimers, so it has two identical subunits (Representation of one <scene name='Sandbox_666/Monomer_structure/4'>subunit</scene>) of 31 kDa, but it is possible to have homotetramers at high concentrations. The constitutive monomers are 276 amino acids long. ''Eco''RI and all the other restriction enzymes show a common structural core, which is a  α/β domain. The constitutive subunits of ''Eco''RI are organized into a single α/β domain (five strands <scene name='Sandbox_666/B_sheet/1'>β</scene> sheet, which is surrounded  by <scene name='Sandbox_666/Helix/1'>two α helices</scene> ). Four of these five β strands are parallel whereas the fourth (β4) is in an anti-parallel orientation to the others.<ref name="B">Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracing.
-Kim YC, Grable JC, Love R, Greene PJ, Rosenberg JM.</ref>
+Kim, Y.C.,  Grable, J.C.,  Love, R.,  Greene, P.J.,  Rosenberg, J.M.,
+Journal: (1990) Science 249: 1307-1309 </ref>
 [[Image:Image1 EcoRI.png |thumb| The topology of EcoRI restriction endonuclease |left| 400px]]