Sandbox 154: Difference between revisions

Line 26:

Domain movement is made possible by rotation about the <scene name='Sandbox_154/2zwh_helix_domains_2/1'> 141-142 and 335-336 peptide bonds</scene>, shown in purple. According to Oda et al.<ref>oda</ref>Domain 2 is believed to tilt 20 degrees and fit itself with Domain 1, thus giving a flatter conformation than the free G-actin. It is not certain whether this flattening occurs before or after ATP hydrolysis.

=== Stability ===

The flattened folded form of F-actin requires different stabilization mechanisms than the free monomeric G-actin form. Stability of the F-actin complex is achieved by a series of <scene name='Sandbox_154/2zwh_saltbridge/1'>salt bridge</scene> formations involving arginine 206, 183, 177 (~~color~~); glutamate 72, aspartate 187, 179 and 4-methyl histidine 73. Additional stability is believed to arise from a break in the interaction between residues <scene name='Sandbox_154/2zwh_leu_val/2'>108-111 and Val165 and Ile175</scene> in the same half of their respective domains to a new interaction between <scene name='Sandbox_154/2zwh_leu_thr/2'>Leu110 and Thr194</scene> where a much greater distance is observed between them<ref>oda</ref>.

The flattened folded form of F-actin requires different stabilization mechanisms than the free monomeric G-actin form. Stability of the F-actin complex is achieved by a series of <scene name='Sandbox_154/2zwh_saltbridge/1'>salt bridge</scene> formations involving arginine 206, 183, 177 (purple); glutamate 72(blue), aspartate 187(green), 179 and 4-methyl histidine 73(yellow). Additional stability is believed to arise from a break in the interaction between residues <scene name='Sandbox_154/2zwh_leu_val/2'>108-111 and Val165 and Ile175</scene> in the same half of their respective domains to a new interaction between <scene name='Sandbox_154/2zwh_leu_thr/2'>Leu110 and Thr194</scene> where a much greater distance is observed between them<ref>oda</ref>.

=== Active Site ===

Sandbox 154: Difference between revisions

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@@ Line 26: / Line 26: @@
 Domain movement is made possible by rotation about the <scene name='Sandbox_154/2zwh_helix_domains_2/1'> 141-142 and 335-336 peptide bonds</scene>, shown in purple. According to Oda et al.<ref>oda</ref>Domain 2 is believed to tilt 20 degrees and fit itself with Domain 1, thus giving a flatter conformation than the free G-actin. It is not certain whether this flattening occurs before or after ATP hydrolysis.
 === Stability ===
-The flattened folded form of F-actin requires different stabilization mechanisms than the free monomeric G-actin form. Stability of the F-actin complex is achieved by a series of <scene name='Sandbox_154/2zwh_saltbridge/1'>salt bridge</scene> formations involving arginine 206, 183, 177 (color); glutamate 72, aspartate 187, 179 and 4-methyl histidine 73. Additional stability is believed to arise from a break in the interaction between residues <scene name='Sandbox_154/2zwh_leu_val/2'>108-111 and Val165 and Ile175</scene> in the same half of their respective domains to a new interaction between <scene name='Sandbox_154/2zwh_leu_thr/2'>Leu110 and Thr194</scene> where a much greater distance is observed between them<ref>oda</ref>.
+The flattened folded form of F-actin requires different stabilization mechanisms than the free monomeric G-actin form. Stability of the F-actin complex is achieved by a series of <scene name='Sandbox_154/2zwh_saltbridge/1'>salt bridge</scene> formations involving arginine 206, 183, 177 (purple); glutamate 72(blue), aspartate 187(green), 179 and 4-methyl histidine 73(yellow). Additional stability is believed to arise from a break in the interaction between residues <scene name='Sandbox_154/2zwh_leu_val/2'>108-111 and Val165 and Ile175</scene> in the same half of their respective domains to a new interaction between <scene name='Sandbox_154/2zwh_leu_thr/2'>Leu110 and Thr194</scene> where a much greater distance is observed between them<ref>oda</ref>.
 === Active Site ===