Clp Protease

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<StructureSection load='1tyf' size='350' side='right' caption='E. coli Clp protease catalytic subunit (PDB entry [[1tyf]])' scene=''>
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<StructureSection load='1tyf' size='350' side='right' caption='E. coli Clp protease catalytic subunit (PDB entry [[1tyf]])' scene='50/508398/Cv/1'>
== Function ==
== Function ==
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* [[Molecular Playground/ClpP]]
* [[Molecular Playground/ClpP]]
* [[Molecular Playground/E. coli ClpP]].
* [[Molecular Playground/E. coli ClpP]].
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'''Clp'''X or '''ATP-dependent Clp protease ATP-binding subunit ClpX''' is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition.<ref>PMID:21736903</ref> For details see [[Molecular Playground/Hexameric ClpX]]
== Structural highlights ==
== Structural highlights ==
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CLP is a heterodimer containing an ATP-binding regulatory subunit A '''ClpA''' or Hsp100 in [[Heat Shock Proteins]] and catalytic subunit P '''ClpP'''. The proteolytic complex is composed of 2 heptameric rings of ClpP flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: ClpA and [[ClpX]].
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CLP is a heterodimer containing an ATP-binding regulatory subunit A '''ClpA''' or Hsp100 in [[Heat Shock Proteins]] and catalytic subunit P '''ClpP'''. The proteolytic complex is composed of <scene name='50/508398/Cv/2'>2 heptameric rings of ClpP</scene> flanked by hexameric rings of ClpA. For full proteolytic activity ClpP must associate with one of two related ATPase subunits: '''ClpA''' and '''ClpX''' or '''ATP-binding Clp protease ATP-binding subunit ClpX'''.
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</StructureSection>
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==3D structures of Clp protease==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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<scene name='45/458468/Cv/4'>ADP binding site</scene> in ''Helicobacter pylori'' ClpX (PDB entry [[1um8]]).<ref>PMID:14514695</ref>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*CLP P subunit
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==3D structures of Clp protease==
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[[Clp protease 3D structures]]
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**[[1tyf]], [[1yg6]] – EcCLP – ''Escherichia coli''<br />
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</StructureSection>
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**[[1yg8]], [[3hln]] - EcCLP (mutant)<br />
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**[[2ds6]] - EcCLP Zinc-binding domain<br />
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**[[1y7o]] – CLP – ''Streptococcus pneumoniae''<br />
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**[[1tg6]] - CLP – human<br />
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**[[2f6i]], [[4gm2]], [[4hnk]] - CLP – ''Plasmodium falciparum''<br />
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**[[2cby]], [[2ce3]], [[2c8t]], [[4u0h]] - MtCLP – ''Mycobacterium tuberculosis''<br />
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**[[3fes]] - CLP – ''Clostridium difficile''<br />
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**[[3ktg]], [[3kth]], [[3tt6]] – BsCLP – ''Bacillus subtilis''<br />
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**[[3p2l]] - CLP – ''Francisella tulerensis''<br />
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**[[3q7h]] - CLP – ''Coxiella burnetii''<br />
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**[[3qwd]], [[3st9]], [[3sta]], [[3v5e]], [[4emm]], [[4mxi]] - SaCLP – ''Staphylococcus aureus''<br />
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**[[3v5i]], [[4emp]] - SaCLP (mutant)<br />
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**[[2zl0]] - HpCLP – ''Helicobacter pylori''<br />
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**[[2zl3]] - HpCLP (mutant)<br />
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**[[4jcq]], [[4jct]], [[4ryf]] – LmCLP – ''Listeria monocytogenes''<br />
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**[[4jcr]] - LmCLP (mutant)<br />
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*''CLP P subunit complex''
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**[[2fzs]], [[3mt6]] - EcCLP + peptide<br />
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**[[2zl2]] - HpCLP + peptide<br />
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**[[2zl4]] - HpCLP (mutant) + peptide<br />
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**[[3kti]], [[3ktj]], [[3ktk]] - BsCLP + peptide<br />
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**[[3tt7]] - BsCLP + DFP<br />
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**[[4u0g]] – MtCLP + ADEP + agonist<br />
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*CLP A subunit and CLP N see [[Heat sock Proteins]] Hsp100
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

E. coli Clp protease catalytic subunit (PDB entry 1tyf)

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References

  1. ↑ Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J Biol Chem. 1990 Jul 25;265(21):12536-45. PMID:2197275
  2. ↑ Baker TA, Sauer RT. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta. 2012 Jan;1823(1):15-28. doi: 10.1016/j.bbamcr.2011.06.007. , Epub 2011 Jun 27. PMID:21736903 doi:http://dx.doi.org/10.1016/j.bbamcr.2011.06.007
  3. ↑ Kim DY, Kim KK. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:14514695 doi:10.1074/jbc.M305882200

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