Sandbox Reserved 325: Difference between revisions
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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 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 | 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'>TextToBeDisplayed</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" />. | ||
The molecular weight of chorismate mutase is 36,000 Da <ref name="pizza" />. Based on the fact that each monomeric subunit has a molecular weight of 18,474 Da, the molecular weight of the molecule supports the theory that it is a dimer <ref name="pizza" />. This is also supported by the fact that all chorismate mutases that occur naturally are either trimers or dimers <ref name="pizza" />. ''M. tuberculosis'' chorismate mutase is similar to the chorismate mutases of yeast and ''E. coli'' in the regards that they all are homodimers <ref name="CMArt2" /> | The molecular weight of chorismate mutase is 36,000 Da <ref name="pizza" />. Based on the fact that each monomeric subunit has a molecular weight of 18,474 Da, the molecular weight of the molecule supports the theory that it is a dimer <ref name="pizza" />. This is also supported by the fact that all chorismate mutases that occur naturally are either trimers or dimers <ref name="pizza" />. ''M. tuberculosis'' chorismate mutase is similar to the chorismate mutases of yeast and ''E. coli'' in the regards that they all are homodimers <ref name="CMArt2" /> | ||
