PDBe 1tyf

X-ray diffraction
2.3Å resolution

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

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo 14-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
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
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 193.32Å b: 102.46Å c: 157.08Å
α: 90° β: 97.8° γ: 90°
R-values:
R R work R free
0.219 0.219 0.292
Expression system: Not provided