Journal:Protein Science:4
From Proteopedia
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===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> | |
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | ''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 |left150px]]''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> | ||
Revision as of 17:36, 18 November 2024
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
