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MtSnf2
From Proteopedia
(Difference between revisions)
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==Myceliophthora thermophila Sucrose Non-Fermenting 2== | ==Myceliophthora thermophila Sucrose Non-Fermenting 2== | ||
| - | <StructureSection load=' | + | <StructureSection load='5hzr' size='340' side='right' caption='Structure of MtSnf2 determined by X-ray crystallography' scene=''> |
| - | The crystal structure of Snf2 (MtSnf2, residues 445-1176) from the yeast '''Myceliophthora thermophila''' was determined, revealing key characteristics of the protein's inactive, ground state conformation. | + | The crystal structure of Snf2 (MtSnf2, residues 445-1176) from the yeast '''Myceliophthora thermophila''' was determined, revealing key characteristics of the protein's inactive, ground state conformation. <ref>PMID: 27399259</ref> |
== Function == | == Function == | ||
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The structure is held in an inactive state by the direct stacking and interaction between the two RecA-like core domains. This interaction twists the essential ATP-binding motifs, Motif I (P loop) and Motif VI (arginine fingers), toward opposite directions, effectively blocking their direct contact and explaining the protein's inactivity in the ground state. The primary interaction occurs at the interface where Core 1, via the &alpha 5 helix, makes hydrophobic contact with <scene name='10/1096884/Val797/1'>V797</scene> from the &beta 7 of the Core 2 domain, burying a solvent-inaccessible surface area. Perturbing this interaction, such as with the T616D V797D double mutation, significantly increases the basal ATPase activity by a factor of 5. Additionally, the post-HSA domain binds to Core 1, specifically interacting with the last helix, which is redefined as the suppressor helix(<scene name='10/1096884/Supph/1'>suppH</scene>). Finally, the C-terminal SnAc domain meanders at the surface of Core 2, covering a large area (over 2,300 angstrom.sq.), and plays a key role in stabilizing the Core 2 domain while making little contact with Core 1. <ref>PMID: 27399259</ref> | The structure is held in an inactive state by the direct stacking and interaction between the two RecA-like core domains. This interaction twists the essential ATP-binding motifs, Motif I (P loop) and Motif VI (arginine fingers), toward opposite directions, effectively blocking their direct contact and explaining the protein's inactivity in the ground state. The primary interaction occurs at the interface where Core 1, via the &alpha 5 helix, makes hydrophobic contact with <scene name='10/1096884/Val797/1'>V797</scene> from the &beta 7 of the Core 2 domain, burying a solvent-inaccessible surface area. Perturbing this interaction, such as with the T616D V797D double mutation, significantly increases the basal ATPase activity by a factor of 5. Additionally, the post-HSA domain binds to Core 1, specifically interacting with the last helix, which is redefined as the suppressor helix(<scene name='10/1096884/Supph/1'>suppH</scene>). Finally, the C-terminal SnAc domain meanders at the surface of Core 2, covering a large area (over 2,300 angstrom.sq.), and plays a key role in stabilizing the Core 2 domain while making little contact with Core 1. <ref>PMID: 27399259</ref> | ||
| - | </StructureSection> | ||
| - | </StructureSection> | ||
== References == | == References == | ||
| - | < | + | <references/> |
Revision as of 13:47, 30 November 2025
Myceliophthora thermophila Sucrose Non-Fermenting 2
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