1g3i | pdb_00001g3i
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CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX
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Structural highlights
FunctionHSLU_HAEIN ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. | ||||||||||||||||||||
This page was last modified 07:22, 7 February 2024.