Clp Protease: Difference between revisions
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For more details see <br /> | For more details see <br /> | ||
* [[Clp protease]] | * [[Clp protease]] | ||
* [[Zinc Fingers]] | |||
* [[Molecular Playground/ClpP]] | * [[Molecular Playground/ClpP]] | ||
* [[Molecular Playground/E. coli ClpP]]. | * [[Molecular Playground/E. coli ClpP]]. | ||
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**[[1tyf]], [[1yg6]] – EcCLP – ''Escherichia coli''<br /> | **[[1tyf]], [[1yg6]] – EcCLP – ''Escherichia coli''<br /> | ||
**[[1yg8]], [[3hln]] - EcCLP (mutant)<br /> | **[[1yg8]], [[3hln]] - EcCLP (mutant)<br /> | ||
**[[2ds6]] - EcCLP Zinc-binding domain<br /> | |||
**[[1y7o]] – CLP – ''Streptococcus pneumoniae''<br /> | **[[1y7o]] – CLP – ''Streptococcus pneumoniae''<br /> | ||
**[[1tg6]] - CLP – human<br /> | **[[1tg6]] - CLP – human<br /> | ||
Revision as of 12:37, 29 February 2016
FunctionClp protease (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins.[1] For more details see Structural highlightsCLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P. |
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3D structures of Clp protease3D structures of Clp protease
Updated on 29-February-2016