Sandbox Reserved 1606: Difference between revisions
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<StructureSection load='5nj3' size='350' side='right' caption='ABCG2 Multidrug Transporter. | <StructureSection load='5nj3' size='350' side='right' caption='ABCG2 Multidrug Transporter. | ||
Green represents residues in monomer A; Purple represents residues in monomer B (PDB Codes: [https://www.rcsb.org/structure/5NJ3 5NJ3] [https://www.rcsb.org/structure/6HBU 6HBU] [https://www.rcsb.org/structure/6HCO 6HCO] [https://www.rcsb.org/structure/6FFC 6FFC])' scene='83/832932/Overall_structure/2'> | Green represents residues in monomer A; Purple represents residues in monomer B. Blue is used to highlight areas of interest in select scenes. (PDB Codes: [https://www.rcsb.org/structure/5NJ3 5NJ3] [https://www.rcsb.org/structure/6HBU 6HBU] [https://www.rcsb.org/structure/6HCO 6HCO] [https://www.rcsb.org/structure/6FFC 6FFC])' scene='83/832932/Overall_structure/2'> | ||
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===ATP Bound and Unbound Conformations=== | ===ATP Bound and Unbound Conformations=== | ||
As an [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC Transporter], ABCG2 exhibits ATPase activity, using the energy of ATP hydrolysis to facilitate transport. After substrate bind in the TMD, one molecule of <scene name='83/832932/Atp_bound_use2/ | As an [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC Transporter], ABCG2 exhibits ATPase activity, using the energy of ATP hydrolysis to facilitate transport. After substrate bind in the TMD, one molecule of <scene name='83/832932/Atp_bound_use2/3'>ATP binds each NBD</scene> (2 molecules of ATP total) causing a conformational change of the overall structure from an <scene name='83/832932/Overall_use_2/3'>inward-facing conformation</scene> to an <scene name='83/832932/Outward_facing_conformation/4'>outward-facing conformation</scene>. One molecule of ATP is hydrolyzed to transport substrates across the cell membrane while the second molecule of ATP is hydrolyzed to reset the transporter to its inward-facing conformation.<ref name="Robey"/> | ||
When ATP binds, α-helices in the NBD <scene name='83/832932/Atp_bound_nbd/2'>rotate</scene> approximately 35° relative to the <scene name='83/832932/Overall_structure_nbd_unbound/2'>inward-facing conformation of NBD</scene>. This shift in the NBD causes slight shifts of α-helices in the TMD; these helices are <scene name='83/832932/Atp_bound_use_tmd/2'>pushed toward each other</scene> relative to the <scene name='83/832932/Overall_structure_tmd_unbound/3'>inward-facing conformation of TMD</scene>. The overall shift from inward-facing to outward-facing promotes the transport of substrates through the transporter.<ref name="Manolaridis"/> | When ATP binds, α-helices in the NBD <scene name='83/832932/Atp_bound_nbd/2'>rotate</scene> approximately 35° relative to the <scene name='83/832932/Overall_structure_nbd_unbound/2'>inward-facing conformation of NBD</scene>. This shift in the NBD causes slight shifts of α-helices in the TMD; these helices are <scene name='83/832932/Atp_bound_use_tmd/2'>pushed toward each other</scene> relative to the <scene name='83/832932/Overall_structure_tmd_unbound/3'>inward-facing conformation of TMD</scene>. The overall shift from inward-facing to outward-facing promotes the transport of substrates through the transporter.<ref name="Manolaridis"/> | ||
