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Clp Protease

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== Structural highlights ==
== Structural highlights ==
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CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P.
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CLP is a heterodimer containing an ATP-binding regulatory subunit A '''ClpA''' 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]].
</StructureSection>
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==3D structures of Clp protease==
==3D structures of Clp protease==

Revision as of 09:28, 31 January 2017

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

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3D structures of Clp protease

Updated on 31-January-2017

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

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Michal Harel, Alexander Berchansky

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