Sandbox Reserved 995: Difference between revisions
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The <scene name='69/691537/Unitb/1'>B’-γ1 subunit</scene>, also known as the regulatory subunit, is not part of the core enzyme but rather a coenzyme that associates with the <scene name='69/691537/Unita/1'>Aα</scene> and <scene name='69/691537/Unitc/1'>Cα</scene> subunits to form the holoenzyme. This subunit resembles the Aα scaffolding subunit structurally; it contains eighteen alpha helixes stacked antiparallel to each other to cause a crescent structure. Of these eighteen alpha helixes eight of them resemble HEAT repeat motifs that resemble repeats found on the Aα subunit. These conserved repeats are located on the, largely hydrophobic, convex side of the B’-γ1 subunit. The hydrophobic residues create a groove to which the Aα subunit loosely associates with, mainly via van der Waal interaction. The concave side of the B’-γ1 subunit consists of a variety of negatively charged amino acid residues, which create an isolated acidic environment. The acid nature of the concave side promotes multiple hydrogen bonds with residues from the Cα subunit. These hydrogen bonds coupled with a multitude of van der Waal interactions results in strong B’-γ1 -Cα subunit association. | The <scene name='69/691537/Unitb/1'>B’-γ1 subunit</scene>, also known as the regulatory subunit, is not part of the core enzyme but rather a coenzyme that associates with the <scene name='69/691537/Unita/1'>Aα</scene> and <scene name='69/691537/Unitc/1'>Cα</scene> subunits to form the holoenzyme. This subunit resembles the Aα scaffolding subunit structurally; it contains eighteen alpha helixes stacked antiparallel to each other to cause a crescent structure. Of these eighteen alpha helixes eight of them resemble HEAT repeat motifs that resemble repeats found on the Aα subunit. These conserved repeats are located on the, largely hydrophobic, convex side of the B’-γ1 subunit. The hydrophobic residues create a groove to which the Aα subunit loosely associates with, mainly via van der Waal interaction. The concave side of the B’-γ1 subunit consists of a variety of negatively charged amino acid residues, which create an isolated acidic environment. The acid nature of the concave side promotes multiple hydrogen bonds with residues from the Cα subunit. These hydrogen bonds coupled with a multitude of van der Waal interactions results in strong B’-γ1 -Cα subunit association. | ||
== HEAT Repeat Motif == | == HEAT Repeat Motif == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
. Campbell, N.A., Reece J.B., Urry, L.A., Cain, M.L., Waserman, S.A., Minorsky, P.V., Jackson, R.B. 2008. Biology, eighth edition. Pearson Benjamin Cummings, San Francisco | |||
