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THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

X-ray diffraction
2.3Å resolution
PDB entry 1tyf coloured by chain, front view.
PDB entry 1tyf coloured by chain, side view.
PDB entry 1tyf coloured by chain, top view.
Source organism: Escherichia coli
Assembly composition:
homo tetradecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Endopeptidase ClpP complex
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Multimeric state: homo tetradecamer
Accessible surface area: 89876.74 Å2
Buried surface area: 57946.49 Å2
Dissociation area: 6,273.11 Å2
Dissociation energy (ΔGdiss): 69.86 kcal/mol
Dissociation entropy (TΔSdiss): 17.1 kcal/mol
Symmetry number: 14
PDBe Complex ID: PDB-CPX-141326
Complex Portal ID: CPX-3178

Macromolecules

ATP-dependent Clp protease proteolytic subunit
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 193 amino acids
Theoretical weight: 21.59 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A6G7 (Residues: 15-207; Coverage: 93%)
Gene names: JW0427, b0437, clpP, lopP
Pfam: Clp protease
InterPro:
CATH: 2-enoyl-CoA Hydratase; Chain A, domain 1
SCOP: Clp protease, ClpP subunit
ATP-dependent Clp protease proteolytic subunit in PDB entry 1tyf, assembly 1, front view.
ATP-dependent Clp protease proteolytic subunit in PDB entry 1tyf, assembly 1, side view.
ATP-dependent Clp protease proteolytic subunit in PDB entry 1tyf, assembly 1, top view.
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