SecA: Difference between revisions
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This is the active site <scene name='Sandbox_158/Scene_1/3'>ADP</scene> with surrounding amino acids shown. | This is the active site <scene name='Sandbox_158/Scene_1/3'>ADP</scene> with surrounding amino acids shown. | ||
Notable finding is that ADP binding to the high-affinity site stabilizes a compact conformation of SecA (ground state) that has low affinity for the SecYEG/membrane<ref name=journal1/>. This result suggests that following ATP hydrolysis, the ADP-bound SecA undergoes retraction from the translocon to complete one reaction cycle. However, the apo (nucleotide free) form of SecA can also exist in a compact conformation with low affinity for the translocon<ref name=journal1/>. Moreover, ADP release from SecA is stimulated by SecYEG/membrane, raising the question whether SecA retraction from the membrane occurs in the ADP-bound form, the apo form, or both<ref name=journal1/>. | |||
==Structure Determination Of SecA-SecY Complexes== | ==Structure Determination Of SecA-SecY Complexes== | ||
