This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Clp Protease

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:10, 24 November 2022) (edit) (undo)
 
(22 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_1tyf| PDB=1tyf | SIZE=400| SCENE= |right|CAPTION=E. coli Clp protease, [[1tyf]] }}
+
<StructureSection load='1tyf' size='350' side='right' caption='E. coli Clp protease catalytic subunit (PDB entry [[1tyf]])' scene='50/508398/Cv/1'>
 +
== Function ==
 +
'''Clp 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.<ref>PMID:2197275</ref><br />
 +
For more details see <br />
 +
* [[Clp protease]]
 +
* [[Zinc Fingers]]
 +
* [[Molecular Playground/ClpP]]
 +
* [[Molecular Playground/E. coli ClpP]].
-
'''Clp 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. CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P. For more details see [[Clp protease]].
+
'''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]]
-
==3D structures of Clp protease==
+
== Structural highlights ==
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
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'''.
-
===CLP P subunit===
+
<scene name='45/458468/Cv/4'>ADP binding site</scene> in ''Helicobacter pylori'' ClpX (PDB entry [[1um8]]).<ref>PMID:14514695</ref>
-
[[1tyf]], [[1yg6]] – EcCLP – ''Escherichia coli''<br />
+
==3D structures of Clp protease==
-
[[1yg8]], [[3hln]] - EcCLP (mutant)<br />
+
[[Clp protease 3D structures]]
-
[[1y7o]] – CLP – ''Streptococcus pneumoniae''<br />
+
-
[[1tg6]] - CLP – human<br />
+
-
[[2f6i]], [[4gm2]], [[4hnk]] - CLP – ''Plasmodium falciparum''<br />
+
-
[[2cby]], [[2ce3]], [[2c8t]] - CLP – ''Mycobacterium tuberculosis''<br />
+
-
[[3fes]] - CLP – ''Clostridium difficile''<br />
+
-
[[3ktg]], [[3kth]], [[3tt6]] – BsCLP – ''Bacillus subtilis''<br />
+
-
[[3p2l]] - CLP – ''Francisella tulerensis''<br />
+
-
[[3q7h]] - CLP – ''Coxiella burnetii''<br />
+
-
[[3qwd]], [[3st9]], [[3sta]], [[3v5e]], [[4emm]] - SaCLP – ''Staphylococcus aureus''<br />
+
-
[[3v5i]], [[4emp]] - SaCLP (mutant)<br />
+
-
[[2zl0]] - HpCLP – ''Helicobacter pylori''<br />
+
-
[[2zl3]] - HpCLP (mutant)<br />
+
-
 
+
-
''CLP P subunit binary complex''
+
-
 
+
-
[[2fzs]], [[3mt6]] - EcCLP + peptide<br />
+
-
[[2zl2]] - HpCLP + peptide<br />
+
-
[[2zl4]] - HpCLP (mutant) + peptide<br />
+
-
[[3kti]], [[3ktj]], [[3ktk]] - BsCLP + peptide<br />
+
-
[[3tt7]] - BsCLP + DFP
+
-
 
+
-
===CLP A subunit===
+
-
[[1k6k]], [[1r6c]] – EcCLP N terminal<br />
+
</StructureSection>
-
[[1ovx]] - EcCLP N terminal - NMR<br />
+
-
[[1ksf]], [[1r6b]] – EcCLP (mutant)<br />
+
-
[[1um8]] – HpCLP
+
-
''CLP A subunit binary complex''
 
-
[[1lzw]], [[1mg9]], [[1mbu]], [[1mbv]], [[1mbx]] – EcCLP + CLP adaptor protein ClpS<br />
+
== References ==
-
[[1r6o]], [[1r6q]] - EcCLP N terminal + CLP adaptor protein ClpS
+
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate


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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Clp_Protease"
Personal tools