Sandbox Reserved 325: Difference between revisions

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*MtCM is a homodimer which has a predominantly α-helical structure.<ref name="pizza" /> There are 10 α-helices spread across the two monomers of chorismate mutase.<ref name="pizza" /> Approximately 86% of the amino acid residues are in the α-helical formations.<ref name="pizza" /> The α-helical structure of *MtCM are similar to the chorismate mutases of ''S. cerevisae'' and ''E. coli''.<ref name="pizza" /> It holds its dimeric state in a protein concentration as low as 5 nM.<ref name="pizza" /> There are no β-sheets present in chorismate mutase.<ref name="CMArt2" />

Chorismate mutase is a homodimer which has a predominantly α-helical structure.<ref name="pizza" /> There are 10 α-helices spread across the two monomers of chorismate mutase.<ref name="pizza" /> Approximately 86% of the amino acid residues are in the α-helical formations.<ref name="pizza" /> The α-helical structure of *MtCM are similar to the chorismate mutases of ''S. cerevisae'' and ''E. coli''.<ref name="pizza" /> It holds its dimeric state in a protein concentration as low as 5 nM.<ref name="pizza" /> There are no β-sheets present in chorismate mutase.<ref name="CMArt2" />

Chorismate has an active site, which is used for the catalysis of the shikimate pathway.<ref name="pizza" /> The <scene name='Sandbox_Reserved_325/Active_site/1'>active site</scene> is made of Arg 49,Lys 60, Arg 72, Thr 105, Glu 109, and Arg 134.<ref name="pizza" /> This active site exists through electrostatic interactions with chorismate and hydrogen bonding between the amino acids <ref name="CMArt2" />. The active site forms within a single chain.<ref name="pizza" /> The active site can form without any help from the second half of the dimer.<ref name="pizza" />

Sandbox Reserved 325: Difference between revisions

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 <Structure load='2f6l' size='300' frame='true' align='left' caption='Chorismate Mutase' scene='Sandbox_Reserved_325/Chainbows/1' />
-*MtCM is a homodimer which has a predominantly α-helical structure.<ref name="pizza" />  There are 10 α-helices spread across the two monomers of chorismate mutase.<ref name="pizza" />  Approximately 86% of the amino acid residues are in the α-helical formations.<ref name="pizza" />  The α-helical structure of *MtCM are similar to the chorismate mutases of ''S. cerevisae'' and ''E. coli''.<ref name="pizza" />  It holds its dimeric state in a protein concentration as low as 5 nM.<ref name="pizza" /> There are no β-sheets present in chorismate mutase.<ref name="CMArt2" />
+ Chorismate mutase is a homodimer which has a predominantly α-helical structure.<ref name="pizza" />  There are 10 α-helices spread across the two monomers of chorismate mutase.<ref name="pizza" />  Approximately 86% of the amino acid residues are in the α-helical formations.<ref name="pizza" />  The α-helical structure of *MtCM are similar to the chorismate mutases of ''S. cerevisae'' and ''E. coli''.<ref name="pizza" />  It holds its dimeric state in a protein concentration as low as 5 nM.<ref name="pizza" /> There are no β-sheets present in chorismate mutase.<ref name="CMArt2" />
 Chorismate has an active site, which is used for the catalysis of the shikimate pathway.<ref name="pizza" />  The <scene name='Sandbox_Reserved_325/Active_site/1'>active site</scene> is made of Arg <sub>49</sub>,Lys <sub>60</sub>, Arg <sub>72</sub>, Thr <sub>105</sub>, Glu <sub>109</sub>, and Arg <sub>134</sub>.<ref name="pizza" /> This active site exists through electrostatic interactions with chorismate and hydrogen bonding between the amino acids <ref name="CMArt2" />.  The active site forms within a single chain.<ref name="pizza" />  The active site can form without any help from the second half of the dimer.<ref name="pizza" />