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Binding of MG132 or Deletion of the Thr Active Sites in HslV Subunits Increases the Affinity of HslV Protease for HslU ATPase and Makes This Interaction Nucleotide-independent
HslVU is an ATP-dependent protease in bacteria consisting of HslV dodecamer and HslU hexamer. Upon ATP binding, HslU ATPase allosterically activates the catalytic function of HslV protease by 1–2 orders of magnitude. However, relatively little is known about the role of HslV in the control of HslU f...
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| Main Authors: | , , , , |
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| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
American Society for Biochemistry and Molecular Biology
2008
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| 主題: | |
| 在線閱讀: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2662256/ https://ncbi.nlm.nih.gov/pubmed/18838376 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M805411200 |
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