Sandbox Reserved 1619: Difference between revisions
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===Lid Complex=== | ===Lid Complex=== | ||
The <scene name='83/832945/Global_lid/1'>lid complex</scene> is the first point of entry and recognition for the substrate. This lid is located within the NCT subunit between Asn55 and Asn435. This lobe of NCT is divided into two separate subunits; the large and small lobes with Phe287 from the large lobe acting as a pivot between them. This <scene name='83/832945/Pivot/2'>Phe is further surrounded by Phe103, Leu171, Phe176, and Ile180</scene> of the small subunit. This congregation of hydrophobic residues composes a greasy pocket that provides an environment for easy structural movement. The lid consists of 5 aromatic residues which are highly involved with stabilizing the closed conformation. In particular, this conformation is stabilized by <scene name='83/832945/Trp164scene/2'>Trp164, which interacts with Pro424, Phe448, and the aliphatic side chain of Gln420</scene>. Once the substrate binds and the lid is opened, a charged, hydrophilic binding pocket is revealed. This pocket contains <scene name='83/832945/Gluandtyr_remake2/1'>Glu333 and Tyr337 surrounded by several charged residues</scene>, and is further involved with substrate binding and recognition once the lid is removed. However, this lid complex is relatively far away from the catalytic site of the enzyme in PS1. Once the substrate binds, the enzyme undergoes a conformational change to shorten this distance, and the rotation of the large lobe in relation to the small lobe reorients the substrate for cleavage by aligning the pocket in NCT to the active site in PS1. <ref name="Bai">PMID:26280335</ref> | The <scene name='83/832945/Global_lid/1'>lid complex</scene> is the first point of entry and recognition for the substrate. <scene name='83/832945/Lidremake2/1'>This lid </scene> is located within the NCT subunit between Asn55 and Asn435. This lobe of NCT is divided into two separate subunits; the large and small lobes with Phe287 from the large lobe acting as a pivot between them. This <scene name='83/832945/Pivot/2'>Phe is further surrounded by Phe103, Leu171, Phe176, and Ile180</scene> of the small subunit. This congregation of hydrophobic residues composes a greasy pocket that provides an environment for easy structural movement. The lid consists of 5 aromatic residues which are highly involved with stabilizing the closed conformation. In particular, this conformation is stabilized by <scene name='83/832945/Trp164scene/2'>Trp164, which interacts with Pro424, Phe448, and the aliphatic side chain of Gln420</scene>. Once the substrate binds and the lid is opened, a charged, hydrophilic binding pocket is revealed. This pocket contains <scene name='83/832945/Gluandtyr_remake2/1'>Glu333 and Tyr337 surrounded by several charged residues</scene>, and is further involved with substrate binding and recognition once the lid is removed. However, this lid complex is relatively far away from the catalytic site of the enzyme in PS1. Once the substrate binds, the enzyme undergoes a conformational change to shorten this distance, and the rotation of the large lobe in relation to the small lobe reorients the substrate for cleavage by aligning the pocket in NCT to the active site in PS1. <ref name="Bai">PMID:26280335</ref> | ||
