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Crystal structure of near full-length hexameric Mycobacterium tuberculosis proteasomal ATPase Mpa in apo form
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Structural highlights
FunctionARC_MYCTA ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. See AlsoContents | ||||||||||||||||||
This page was last modified 12:42, 6 March 2024.