Sandbox 154: Difference between revisions
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=== Active Site === | === Active Site === | ||
Upon actin binding on the plus end of the actin filament, the ATPase function is activated. The conformational change from G- to F- actin promotes the catalytic activity because of the 20 degree shift leading to a more closed binding site; this conformational change is stabilized also by the diagonal subdomain interaction between Leu110 and Thr194. | |||
Upon binding changes, the Gln137 residue of actin is moved closer to the ATP-Ca2+ ligand. Gln137 holds a water molecule, and placing it in close proximity to ATP allows for the gamma-phosphate to become cleaved. Release of the inorganic phosphate occurs via the conformational change of the flexible "D-loop" into an ordered alpha-helix<ref>graceffa</ref>. | |||
=== Polymer F-actin === | === Polymer F-actin === | ||
