Sandbox Reserved 325: Difference between revisions

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Chorismate mutase is a homodimer which has an ~~all-~~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 ''M. tuberculosis'' chorismate mustase 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 an 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 ''M. tuberculosis'' chorismate mustase 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 active site 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="CMW2" />. 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='Insert caption here' scene='Sandbox_Reserved_325/Chainbows/1' />
-Chorismate mutase is a homodimer which has an all-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 ''M. tuberculosis'' chorismate mustase 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 an 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 ''M. tuberculosis'' chorismate mustase 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 active site 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="CMW2" />.  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" />.