Sandbox 154: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Melissa Chow (talk | contribs) |
Melissa Chow (talk | contribs) |
||
| Line 16: | Line 16: | ||
== Structure == | == Structure == | ||
<applet load='2zwh' size='222' color='black' frame='true' align='left' caption='Filamentous Actin (F-actin)' scene='Sandbox_154/2zwh_black_domains/1'/> | |||
=== Domains of F-actin Unit === | === Domains of F-actin Unit === | ||
Structure of a unit of F-actin with domains from a single polypeptide chain. Note the cleft between the two domains houses the nucleotide phosphate ligand and the Ca2+ metal ion ligand. | Structure of a unit of F-actin with domains from a single polypeptide chain. Note the cleft between the two domains houses the nucleotide phosphate ligand and the Ca2+ metal ion ligand. | ||
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. | 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. | ||
