HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis.

Abstract

HslVU is a bacterial ATP-dependent protease distantly related to eukaryotic proteasomes consisting of hexameric HslU ATPase and dodecameric HslV protease. As a homolog of the 20 S proteasome beta-subunits, HslV also uses the N-terminal threonine as the active site residue. However, unlike the proteasome that has only 6 active sites among the 14 beta… (More)
DOI: 10.1074/jbc.M109.045807

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Cite this paper

@article{Lee2009HslVUAP, title={HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis.}, author={Jung Wook Lee and Eunyong Park and Min Sun Jeong and Young Joo Jeon and Soo Hyun Eom and Jae Hong Seol and Chin Ha Chung}, journal={The Journal of biological chemistry}, year={2009}, volume={284 48}, pages={33475-84} }