Sandbox 154: Difference between revisions
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=== Domains of F-actin Unit === | === Domains of F-actin Unit === | ||
The structure of a single unit of F-actin arises from one polypeptide chain with two domains, as observed by the figure on the left. The nucleotide binding cleft, site of ATP hydrolysis, can be observed between the two domains. Movement of the domains allows for the open and closed F-actin conformations. | |||
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. | 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., during the transition from G- to F- actin, Domain 2 is believed to tilt 20°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<ref name="oda" />. | ||
=== Stability === | === Stability === | ||
