Sandbox Reserved 1094: Difference between revisions

Line 94:

The dimer is very extend compared to the monomer with a size of 112Å.

The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a β-half-barrel ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are three salt bridges, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>

The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a <scene name='82/829347/Betahalfbarrel/1'>β-half-barrel</scene> ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are <scene name='82/829347/Saltbridges/1'>three salt bridges</scene>, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>

The active site of the enzyme is contained in each monomer but the dimeric form is necessary to the biological activity indeed it confers the stability in aqueous medium.

Sandbox Reserved 1094: Difference between revisions

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@@ Line 94: / Line 94: @@
 The dimer is very extend compared to the monomer with a size of 112Å.
-The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a β-half-barrel ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are three salt bridges, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>
+The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a <scene name='82/829347/Betahalfbarrel/1'>β-half-barrel</scene> ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are <scene name='82/829347/Saltbridges/1'>three salt bridges</scene>, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>
 The active site of the enzyme is contained in each monomer but the dimeric form is necessary to the biological activity indeed it confers the stability in aqueous medium.