Journal:Protein Science:4: Difference between revisions
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<StructureSection load='' size='340' side='right' scene='10/1063617/009_figu_5b_png/3' caption='Acetylcholinesterase highlighting the 4A/3B motif'> | <StructureSection load='' size='340' side='right' scene='10/1063617/009_figu_5b_png/3' caption='Acetylcholinesterase highlighting the 4A/3B motif'> | ||
===Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?=== | ===Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?=== | ||
<br /><big>Lushchekina, Weiner, Ashani, Emrizal, Firdaus-Raih, Silman & Sussman</big><ref>PMID: 39548604</ref> | <br /><big>Lushchekina, Weiner, Ashani, Emrizal, Firdaus-Raih, Silman & Sussman</big><ref>PMID: 39548604</ref> | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
[[Image:2024_Lushchekina_Prot_Sci_x.jpg| thumb |left|150px|For a divalent cation, it is hard to unbind from structural motifs composed of 4 acidic residues (4A). However, it is much easier if the motif is surrounded by 3 basic residues (4A/3B).]]''Torpedo californica'' acetylcholinesterase (''Tc''AChE) contains a unique 4D motif composed of four aspartate residues that can bind divalent metal cations (like Ca²⁺, Mg²⁺, Mn²⁺), significantly increasing the enzyme’s thermal stability. Despite the electrostatic repulsion expected between these aspartates, structural analysis shows that the enzyme's conformation remains stable | [[Image:2024_Lushchekina_Prot_Sci_x.jpg| thumb |left|150px|For a divalent cation, it is hard to unbind from structural motifs composed of 4 acidic residues (4A). However, it is much easier if the motif is surrounded by 3 basic residues (4A/3B).]] | ||
[[Image:2024_Lushchekina_Prot_Sci_x.jpg| thumb |left|150px|For a divalent cation, it is hard to unbind from structural motifs composed of 4 acidic residues (4A). However, it is much easier if the motif is surrounded by 3 basic residues (4A/3B). [https://doi.org/10.1002/pro.5206]] | |||
''Torpedo californica'' acetylcholinesterase (''Tc''AChE) contains a unique 4D motif composed of four aspartate residues that can bind divalent metal cations (like Ca²⁺, Mg²⁺, Mn²⁺), significantly increasing the enzyme’s thermal stability. Despite the electrostatic repulsion expected between these aspartates, structural analysis shows that the enzyme's conformation remains stable | |||
<scene name='10/1063617/009_fig_metal_tcache_lab_png/2'>with</scene> or <scene name='10/1063617/009_fig_apo_tcache_lab_png/2'>without</scene> bound cations as seen in an <scene name='10/1063617/009_fig_metal_apo_tcache_lab/2'>overlay</scene> the two states and an <jmol> | <scene name='10/1063617/009_fig_metal_tcache_lab_png/2'>with</scene> or <scene name='10/1063617/009_fig_apo_tcache_lab_png/2'>without</scene> bound cations as seen in an <scene name='10/1063617/009_fig_metal_apo_tcache_lab/2'>overlay</scene> the two states and an <jmol> | ||
<jmolButton> | <jmolButton> | ||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For additional details please see I3DC.
